The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima (193 views)
Acta Crystallogr F Struct Biol Commun (ISSN: 2053-230xlinking), 2019 Nov 1; 75(Pt11): 707-713.
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Paper type: Journal Article
Impact factor: 0.968, 5-year impact factor: 0.887
Url: https://pubmed.ncbi.nlm.nih.gov/31702584/
Keywords: Thermotoga Maritima, Arginine-Binding Protein, Domain Swapping, Proline Residue, Protein Oligomerization, Protein Structure Dynamics, Protein Structure–stability, Amino Acid Sequence , Arginine Metabolism , Bacterial Proteins Chemistry Genetics Metabolism , Crystallization , Mutation Genetics , Protein Binding , Structural Homology, Thermotoga Maritima Metabolism
Affiliations:
AIC School Crystallographic Information Fiesta 2019, Naples, Italy.
References:
Not available.
Acta Crystallogr F Struct Biol Commun (ISSN: 2053-230xlinking), 2019 Nov 1; 75(Pt11): 707-713.
Export to BibTeX Export to EndNote
Paper type: Journal Article
Impact factor: 0.968, 5-year impact factor: 0.887
Url: https://pubmed.ncbi.nlm.nih.gov/31702584/
Keywords: Thermotoga Maritima, Arginine-Binding Protein, Domain Swapping, Proline Residue, Protein Oligomerization, Protein Structure Dynamics, Protein Structure–stability, Amino Acid Sequence , Arginine Metabolism , Bacterial Proteins Chemistry Genetics Metabolism , Crystallization , Mutation Genetics , Protein Binding , Structural Homology, Thermotoga Maritima Metabolism
Affiliations:
AIC School Crystallographic Information Fiesta 2019, Naples, Italy.
References:
Not available.
The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima
Domain swapping is a widespread oligomerization process that is observed in a large variety of protein families. In the large superfamily of substrate-binding proteins, non-monomeric members have rarely been reported. The arginine-binding protein from Thermotoga maritima (TmArgBP), a protein endowed with a number of unusual properties, presents a domain-swapped structure in its dimeric native state in which the two polypeptide chains mutually exchange their C-terminal helices. It has previously been shown that mutations in the region connecting the last two helices of the TmArgBP structure lead to the formation of a variety of oligomeric states (monomers, dimers, trimers and larger aggregates). With the aim of defining the structural determinants of domain swapping in TmArgBP, the monomeric form of the P235GK mutant has been structurally characterized. Analysis of this arginine-bound structure indicates that it consists of a closed monomer with its C-terminal helix folded against the rest of the protein, as typically observed for substrate-binding proteins. Notably, the two terminal helices are joined by a single nonhelical residue (Gly235). Collectively, the present findings indicate that extending the hinge region and conferring it with more conformational freedom makes the formation of a closed TmArgBP monomer possible. On the other hand, the short connection between the helices may explain the tendency of the protein to also adopt alternative oligomeric states (dimers, trimers and larger aggregates). The data reported here highlight the importance of evolutionary control to avoid the uncontrolled formation of heterogeneous and potentially harmful oligomeric species through domain swapping.
Domain swapping is a widespread oligomerization process that is observed in a large variety of protein families. In the large superfamily of substrate-binding proteins, non-monomeric members have rarely been reported. The arginine-binding protein from Thermotoga maritima (TmArgBP), a protein endowed with a number of unusual properties, presents a domain-swapped structure in its dimeric native state in which the two polypeptide chains mutually exchange their C-terminal helices. It has previously been shown that mutations in the region connecting the last two helices of the TmArgBP structure lead to the formation of a variety of oligomeric states (monomers, dimers, trimers and larger aggregates). With the aim of defining the structural determinants of domain swapping in TmArgBP, the monomeric form of the P235GK mutant has been structurally characterized. Analysis of this arginine-bound structure indicates that it consists of a closed monomer with its C-terminal helix folded against the rest of the protein, as typically observed for substrate-binding proteins. Notably, the two terminal helices are joined by a single nonhelical residue (Gly235). Collectively, the present findings indicate that extending the hinge region and conferring it with more conformational freedom makes the formation of a closed TmArgBP monomer possible. On the other hand, the short connection between the helices may explain the tendency of the protein to also adopt alternative oligomeric states (dimers, trimers and larger aggregates). The data reported here highlight the importance of evolutionary control to avoid the uncontrolled formation of heterogeneous and potentially harmful oligomeric species through domain swapping.
The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima
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The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima
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Cozzolino S, Balasco N, Vigorita M, Ruggiero A, Smaldone G, Del Vecchio P, Vitagliano L, Graziano G
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* Guanidinium binding to proteins: The intriguing effects on the D1 and D2 domains of Thermotoga maritima Arginine Binding Protein and a comprehensive analysis of the Protein Data Bank (113 views)
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View Export to BibTeX Export to EndNote
Smaldone G, Ruggiero A, Balasco N, Vitagliano L
* Development of a Protein Scaffold for Arginine Sensing Generated through the Dissection of the Arginine-Binding Protein from Thermotoga maritima (209 views)
Int J Mol Sc (ISSN: 1422-0067linking, 1422-0067electronic, 1661-6596), 2020 Oct 12; 21(20): N/D-N/D.
Impact Factor: 4.556
View Export to BibTeX Export to EndNote
Esposito L, Donnarumma F, Ruggiero A, Leone S, Vitagliano L, Picone D
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Impact Factor: 4.784
View Export to BibTeX Export to EndNote
Balasco N, Smaldone G, Vigorita M, Del Vecchio P, Graziano G, Ruggiero A, Vitagliano L
* The characterization of Thermotoga maritima Arginine Binding Protein variants demonstrates that minimal local strains have an important impact on protein stability (208 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2019 Apr 29; 9(1): 6617-6617.
Impact Factor: 5.078
View Export to BibTeX Export to EndNote
Smaldone G, Balasco N, Vigorita M, Ruggiero A, Cozzolino S, Berisio R, Del Vecchio P, Graziano G, Vitagliano L
* Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection (257 views)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Nov; 119: 758-769.
Impact Factor: 3.909
View Export to BibTeX Export to EndNote
Smaldone G, Berisio R, Balasco N, D'Auria S, Vitagliano L, Ruggiero A
* Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization (343 views)
Bba-Gen Subjects (ISSN: 1570-9639print, 1570-9639linking, 0005-2728), 2018 May 31; 1866(9): 952-962.
Impact Factor: 2.773
View Export to BibTeX Export to EndNote
Smaldone G, Vigorita M, Ruggiero A, Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L
* Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein (590 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2016 Jul; 1864(7): 814-824.
Impact Factor: 4.932
View Export to BibTeX Export to EndNote
Smaldone G, Pirone L, Pedone E, Marlovits T, Vitagliano L, Ciccarelli L
* The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states (383 views) (PDF 59 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468), 2016 Jun; 590(11): 1663-1671.
Impact Factor: 3.623
View Export to BibTeX Export to EndNote
Ruggiero A, Dattelbaum JD, Staiano M, Berisio R, D'Auria S, Vitagliano L
* A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima (649 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2014 May 15; 9(5): e96560-e96560.
Impact Factor: 3.234
View Export to BibTeX Export to EndNote
Sica F, Pica A, Merlino A, Russo Krauss I, Ercole C, Picone D
* The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer (397 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013 Nov 29; 587(23): 3755-3762.
Impact Factor: 3.341
View Export to BibTeX Export to EndNote
Pica A, Merlino A, Buell AK, Knowles TJ, Pizzo E, D'Alessio G, Sica F, Mazzarella L
* Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase (1255 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Oct; 69: 2116-2123.
Impact Factor: 7.232
View Export to BibTeX Export to EndNote
Merlino A, Picone D, Ercole C, Balsamo A, Sica F
* Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease (387 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2012 May; 94(5): 1108-1118.
Impact Factor: 3.142
View Export to BibTeX Export to EndNote
Ruggiero A, Dattelbaum JD, Pennacchio A, Iozzino L, Staiano M, Luchansky MS, Der BS, Berisio R, D'Auria S, Vitagliano L
* Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein (677 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2011 Nov 1; 67(11): 1462-1465.
Impact Factor: 0.506
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
* Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin (542 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Luchansky MS, Der BS, D'Auria S, Pocsfalvi G, Iozzino L, Marasco D, Dattelbaum JD
* Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima (869 views)
Molecular Biosystems (ISSN: 1742-206x), 2010; 6(1): 142-151.
Impact Factor: 3.825
View Export to BibTeX Export to EndNote
Merlino A, Russo Krauss I, Perillo M, Mattia CA, Ercole C, Picone D, Vergara A, Sica F
* Toward an Antitumor Form of Bovine Pancreatic Ribonuclease: The Crystal Structure of Three Noncovalent Dimeric Mutants (498 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1029-1037.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
Merlino A, Avella G, Di Gaetano S, Arciello A, Piccoli R, Mazzarella L, Sica F
* Structural features for the mechanism of antitumor action of a dimeric human pancreatic ribonuclease variant (424 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic, 0961-8368linking), 2009 Jan; 18(1): 50-57.
Impact Factor: 2.937
View Export to BibTeX Export to EndNote
Merlino A, Ercole C, Picone D, Pizzo E, Mazzarella L, Sica F
* The buried diversity of bovine seminal ribonuclease: Shape and cytotoxicity of the swapped non-covalent form of the enzyme (741 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2008 Feb 15; 376(2): 427-437.
Impact Factor: 4.146
View Export to BibTeX Export to EndNote
Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G
* On the thermal stability of the two dimeric forms of ribonuclease (604 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005 Jul 1; 116(2): 89-95.
Impact Factor: 1.925
View Export to BibTeX Export to EndNote
Naddeo M, Vitagliano L, Russo A, Gotte G, D'Alessio G, Sorrentino S
* Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor (462 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 May 9; 579(12): 2663-2668.
Impact Factor: 3.415
View Export to BibTeX Export to EndNote
Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (535 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Esposito L, Daggett V
* Insight into ribonuclease A domain swapping by molecular dynamics unfolding simulations (626 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2005 Mar 8; 44(9): 3358-3368.
Impact Factor: 3.848
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Alterio V, Mandrich L, Rossi M, Manco G, Pedone C
* The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family (1052 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2004 Oct 8; 343(1): 137-146.
Impact Factor: 5.542
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (437 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Berisio R, Sica F, De Lorenzo C, Di Fiore A, Piccoli R, Zagari A, Mazzarella L
* Crystal Structure Of The Dimeric Un-Swapped Form Of Bovine Seminal Ribonuclease (443 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2003 Nov 6; 554(1-2): 105-110.
Impact Factor: 3.609
View Export to BibTeX Export to EndNote
Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (419 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
View Export to BibTeX Export to EndNote
Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease (527 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 29; 293(3): 569-577.
Impact Factor: 5.501
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Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state (358 views)
J Cryst Growth (ISSN: 0022-0248), 1999; 196(2-4): 305-312.
Impact Factor: 1.492
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Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine (549 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
Impact Factor: 4.44
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Adinolfi S, Piccoli R, Sica F, Mazzarella L
BS-RNase tetramers: An example of domain-swapped oligomers (539 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 1996 Dec 2; 398(2-3): 326-332.
Impact Factor: 3.504
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30 Records (30 excluding Abstracts).
Total impact factor: 115.738 (115.738 excluding Abstracts).
Total 5 year impact factor: 109.631 (109.631 excluding Abstracts).
Total impact factor: 115.738 (115.738 excluding Abstracts).
Total 5 year impact factor: 109.631 (109.631 excluding Abstracts).
193 views. Last view on Friday 13 September 2024, 14:20:09
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