Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection (274 views)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Nov; 119: 758-769.
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Paper type: Journal Article,
Impact factor: 3.909, 5-year impact factor: 3.929
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Keywords: Biosensor , Diagnostic Tool , Differential Scanning Calorimetry , Domain-Domain Communication , Protein Dissection , Protein Structure-Stability, Amino Acid Sequence , Arginine Metabolism , Carrier Proteins Chemistry Metabolism , Models, Molecular , Protein Binding , Protein Conformation , Protein Interaction Domains And Motifs , Structure-Activity Relationship , Thermodynamics , Thermotoga Maritima Metabolism,
Affiliations:
*** IBB - CNR ***
IRCCS SDN, Via Emanuele Gianturco 113, 80143 Napoli, Italy. Electronic address: gsmaldone@sdn-napoli.it.
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
Department of Sciences and Technologies, Universita del Sannio, via Port'arsa 11, 82100 Benevento, Italy.
Department of Chemical Sciences, University of Naples Federico II, via Cintia, 80126 Napoli, Italy.
References:
Not available.
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Nov; 119: 758-769.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.909, 5-year impact factor: 3.929
Url: Not available.
Keywords: Biosensor , Diagnostic Tool , Differential Scanning Calorimetry , Domain-Domain Communication , Protein Dissection , Protein Structure-Stability, Amino Acid Sequence , Arginine Metabolism , Carrier Proteins Chemistry Metabolism , Models, Molecular , Protein Binding , Protein Conformation , Protein Interaction Domains And Motifs , Structure-Activity Relationship , Thermodynamics , Thermotoga Maritima Metabolism,
Affiliations:
*** IBB - CNR ***
IRCCS SDN, Via Emanuele Gianturco 113, 80143 Napoli, Italy. Electronic address: gsmaldone@sdn-napoli.it.
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
Department of Sciences and Technologies, Universita del Sannio, via Port'arsa 11, 82100 Benevento, Italy.
Department of Chemical Sciences, University of Naples Federico II, via Cintia, 80126 Napoli, Italy.
References:
Not available.
Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection
Substrate binding proteins represent a large protein family that plays fundamental roles in selective transportation of metabolites across membrane. The function of these proteins relies on the relative motions of their two domains. Insights into domain communication in this class of proteins have been here collected using Thermotoga maritima Arginine Binding Protein (TmArgBP) as model system. TmArgBP was dissected into two domains (D1 and D2) that were exhaustively characterized using a repertoire of different experimental and computational techniques. Indeed, stability, crystalline structure, ability to recognize the arginine substrate, and dynamics of the two individual domains have been here studied. Present data demonstrate that, although in the parent protein both D1 and D2 cooperate for the arginine anchoring; only D1 is intrinsically able to bind the substrate. The implications of this finding on the mechanism of arginine binding and release by TmArgBP have been discussed. Interestingly, both D1 and D2 retain the remarkable thermal/chemical stability of the parent protein. The analysis of the structural and dynamic properties of TmArgBP and of the individual domains highlights possible routes of domain communication. Finally, this study generated two interesting molecular tools, the two stable isolated domains that could be used in future investigations.
Substrate binding proteins represent a large protein family that plays fundamental roles in selective transportation of metabolites across membrane. The function of these proteins relies on the relative motions of their two domains. Insights into domain communication in this class of proteins have been here collected using Thermotoga maritima Arginine Binding Protein (TmArgBP) as model system. TmArgBP was dissected into two domains (D1 and D2) that were exhaustively characterized using a repertoire of different experimental and computational techniques. Indeed, stability, crystalline structure, ability to recognize the arginine substrate, and dynamics of the two individual domains have been here studied. Present data demonstrate that, although in the parent protein both D1 and D2 cooperate for the arginine anchoring; only D1 is intrinsically able to bind the substrate. The implications of this finding on the mechanism of arginine binding and release by TmArgBP have been discussed. Interestingly, both D1 and D2 retain the remarkable thermal/chemical stability of the parent protein. The analysis of the structural and dynamic properties of TmArgBP and of the individual domains highlights possible routes of domain communication. Finally, this study generated two interesting molecular tools, the two stable isolated domains that could be used in future investigations.
Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection
Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 4.932
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.603
View Export to BibTeX Export to EndNote
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Impact Factor: 2.631
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 1.595
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (736 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 7; 8(7): 744-756.
Impact Factor: 3.446
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Pappalardo G, Milardi D, Magrì A, Attanasio F, Impellizzeri G, La Rosa C, Grasso D, Rizzarelli E
* Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (782 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(36): 10204-10215.
Impact Factor: 5.33
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Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
* Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (486 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2007; 46(42): 7993-7995.
Impact Factor: 10.031
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Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
* Role of electrostatics in the thermal stability of ubiquitin: A combined DSC and MM study (334 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006 Nov; 86(2): 311-314.
Impact Factor: 1.438
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Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G
* On the thermal stability of the two dimeric forms of ribonuclease (611 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005 Jul 1; 116(2): 89-95.
Impact Factor: 1.925
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Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (346 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
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La Rosa C, Milardi D, Amato E, Pappalardo M, Grasso D
* Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly (672 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2005 Mar 1; 435(1): 182-189.
Impact Factor: 3.152
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Romano M, Amato B, Markabaoui K, Tamburrini O, Salvatore M
* Multidetector row computed tomographic angiography of the abdominal aorta and lower limbs arteries: A new diagnostic tool in patients with peripheral arterial occlusive disease (433 views)
Minerva Cardioangiol, 2004 Feb; 52(1): 9-17.
Impact Factor: 0.481
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (375 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
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Milardi D, Grasso DM, Verbeet MP, Canters GW, La Rosa C
* Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions (454 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2003 Jun 1; 414(1): 121-127.
Impact Factor: 2.338
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Guzzi R, Milardi D, La Rosa C, Grasso D, Verbeet MP, Canters GW, Sportelli L
* The effect of copper/zinc replacement on the folding free energy of wild type and Cys3Ala/Cys26Ala azurin (406 views)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2003 Jan 15; 31(4-5): 163-170.
Impact Factor: 1.427
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Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
* Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study (568 views)
New J Chem (ISSN: 1144-0546), 2003; 27(2): 359-364.
Impact Factor: 2.272
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Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (421 views)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (417 views)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
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Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins (1089 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
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36 Records (36 excluding Abstracts).
Total impact factor: 135.205 (135.205 excluding Abstracts).
Total 5 year impact factor: 134.507 (134.507 excluding Abstracts).
Total impact factor: 135.205 (135.205 excluding Abstracts).
Total 5 year impact factor: 134.507 (134.507 excluding Abstracts).
274 views. Last view on Sunday 13 October 2024, 7:19:12
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