Ribosomal crystallography: Peptide bond formation and its inhibition
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Ribosomal crystallography: Peptide bond formation and its inhibition
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641 views
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D,
Berisio R
, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print)
,
2003 Sep;
70(1): 19-41.
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Paper type:
Journal Article,
Impact factor:
2.733,
5-year impact factor:
2.675
Url:
http://www.scopus.com/inward/record.url?eid=2-s2.0-10744220564&partnerID=40&md5=b319d9712d7d3360f8811658e7eb404e
Keywords:
Elongation Arrest, Peptide-Bond Formation, Ribosomes, Translocation, Tunnel Gating, Biosynthesis, Polypeptides, Proteins, Cellular Organelles, Crystallography, Antibiotic Agent, Azithromycin, Chloramphenicol, Clarithromycin, Clindamycin, Erythromycin, Ketolide, Lincomycin, Macrolide, Nucleotide, Protein Subunit, Protein Synthesis Inhibitor, Puromycin, Ribosome Rna, Roxithromycin, Sparsomycin, Tetracycline, Transfer Rna, Troleandomycin, Article, Binding Site, Catalysis, Cell Organelle, Channel Gating, Enzyme Active Site, Enzyme Substrate, Eubacterium, Genetic Code, Geometry, Molecular Dynamics, Molecular Weight, Orientation, Process Monitoring, Protein Assembly, Protein Binding, Protein Rna Binding, Protein Structure, Protein Synthesis Inhibition, Reaction Analysis, Ribosome Subunit, Rna Translation, Rna Transport, Rotation, Anti-Bacterial Agents, Catalytic Domain, X-Ray, Models, Molecular Conformation, Nucleic Acid Conformation, Peptidyl Transferases, Protein Conformation, Bacteria (microorganisms),
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
FB Biologie, Chemie, Pharmazie, Frei Uni. Berlin, 14195 Berlin, Germany
Max-Planck-Inst. for Molec. Genet., 14195 Berlin, Germany
Inst. of Biostructure and Bioimage, CNR, 80138 Napoli, Italy
References:
Not available.
Ribosomal crystallography: Peptide bond formation and its inhibition
Ribosomes, the universal cellular organelles catalyzing the translation of genetic code into proteins, are protein/RNA assemblies, of a molecular weight 2.5 mega Daltons or higher. They are built of two subunits that associate for performing protein biosynthesis. The large subunit creates the peptide bond and provides the path for emerging proteins. The small has key roles in initiating the process and controlling its fidelity. Crystallographic studies on complexes of the small and the large eubacterial ribosomal subunits with substrate analogs, antibiotics, and inhibitors confirmed that the ribosomal RNA governs most of its activities, and indicated that the main catalytic contribution of the ribosome is the precise positioning and alignment of its substrates, the tRNA molecules. A symmetry-related region of a significant size, containing about two hundred nucleotides, was revealed in all known structures of the large ribosomal subunit, despite the asymmetric nature of the ribosome. The symmetry rotation axis, identified in the middle of the peptide-bond formation site, coincides with the bond connecting the tRNA double-helical features with its single-stranded 3′ end, which is the moiety carrying the amino acids. This thus implies sovereign movements of tRNA features and suggests that tRNA translocation involves a rotatory motion within the ribosomal active site. This motion is guided and anchored by ribosomal nucleotides belonging to the active site walls, and results in geometry suitable for peptide-bond formation with no significant rearrangements. The sole geometrical requirement for this proposed mechanism is that the initial P-site tRNA adopts the flipped orientation. The rotatory motion is the major component of unified machinery for peptide-bond formation, translocation, and nascent protein progression, since its spiral nature ensures the entrance of the nascent peptide into the ribosomal exit tunnel. This tunnel, assumed to be a passive path for the growing chains, was found to be involved dynamically in gating and discrimination. © 2003 Wiley Periodicals, Inc.
Ribosomal crystallography: Peptide bond formation and its inhibition
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Agmon I, Auerbach T, Baram D, Bartels H, Bashan A,
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)
Chembiochem
,
2003 Jun;
270(12): 2543-2556.
Impact Factor:
3.06
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Berisio R
, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
*
Structural insight into the role of the ribosomal tunnel in cellular regulation
(
481 views
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Nat Struct Biol (ISSN: 1072-8368)
,
2003 May;
10(5): 366-370.
Impact Factor:
11.579
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Isernia C, Bucci E,
Leone M
,
Zaccaro L
, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B,
Pedone C
, Pedone PV, Fattorusso R
*
NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein
(
567 views
)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic)
,
2003 Mar 3;
4(2-3): 171-180.
Impact Factor:
3.992
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Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J,
Berisio R
, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
*
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
(
540 views
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Mol Cell (ISSN: 1097-2765, 1097-4164)
,
2003 Jan;
11(1): 91-102.
Impact Factor:
16.835
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Peggion C, Formaggio F, Crisma M, Toniolo C, Jimenez AI, Cativiela C, Kaptein B, Broxterman QB, Saviano M, Benedetti E
*
Folding of peptides characterized by c3Val, a highly constrained analogue of valine
(
517 views
)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print)
,
2003;
68(2): 178-191.
Impact Factor:
2.733
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Fassina G,
Ruvo M
, Palombo G, Verdoliva A, Marino M
*
Novel ligands for the affinity-chromatographic purification of antibodies
(
1485 views
)
J Biochem Biophys Methods (ISSN: 0165-022x, 0165-022xlinking)
,
2001 Oct 30;
49(1-3): 481-490.
Impact Factor:
1.218
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De Falco S, Ruvoletto MG, Verdoliva A,
Ruvo M
, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
*
Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells
(
767 views
)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking)
,
2001 Sep 28;
276(39): 36613-36623.
Impact Factor:
7.258
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Romanelli A
, Garella I,
Menchise V
, Iacovino R, Saviano M, Montesarchio D, Didierjean C, Lello PD,
Rossi F
, Benedetti E
*
Crystal-state conformation of Cα, α-dialkylated peptides containing chiral β-homo-residues
(
616 views
)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print)
,
2001;
7(1): 15-26.
Impact Factor:
1.451
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Durante M,
Cella L
, Furusawa Y, George K, Gialanella G, Grossi G, Pugliese M, Saito M, Yang TC
The effect of track structure on the induction of chromosomal aberrations in murine cells
(
812 views
)
Int J Radiat Biol International Journal Of Radiation Biology (ISSN: 0955-3002)
,
1998 Mar;
73(3): 253-262.
Impact Factor:
2.579
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Caraglia M, Tagliaferri P, Correale P, Genua G, Pinto A,
Del Vecchio S
, Esposito G, Bianco AR
Cytosine arabinoside increases the binding of 125I-labelled epidermal growth factor and 125I-transferrin and enhances the in vitro targeting of human tumour cells with anti-(growth factor receptor) mAb
(
295 views
)
Cancer Immunol Immunother (ISSN: 0340-7004linking)
,
1993 Aug;
37 (3 ): 150-156.
Impact Factor:
4.293
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Oliva A, Della Ragione F, Fratta M, Marrone G,
Palumbo R
, Zappia V
Effect of retinoic acid on osteocalcin gene expression in human osteoblasts
(
350 views
)
Biochem Biophys Res Commun (ISSN: 0006-291xprint, 0006-291xlinking)
,
1993 Mar 31;
191(3): 908-914.
Impact Factor:
2.671
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Oliva A, Marrone G, Della Ragione F, Riccio V,
Palumbo R
, Rossano F, Zappia V
Isolation and characterization of human embryonic osteoblasts
(
490 views
)
Calcif Tissue Int (ISSN: 0171-967xprint, 0171-967xlinking)
,
1992 Nov;
51(5): 356-362.
Impact Factor:
2.364
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Margotta V,
Fonti R
, Palladini G, Filoni S, Lauro GM
Transient expression of glial-fibrillary acidic protein (GFAP) in the ependyma of the regenerating spinal cord in adult newts
(
528 views
)
Journal Fur Hirnforschung (ISSN: 0021-8359)
,
1991;
32(4): 485-490.
Impact Factor:
0
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54
Records (
53
excluding Abstracts).
Total impact factor:
192.009
(
190.071
excluding Abstracts).
Total 5 year impact factor:
206.342
(
201.372
excluding Abstracts).
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