1ok7

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{{STRUCTURE_1ok7| PDB=1ok7 | SCENE= }}
{{STRUCTURE_1ok7| PDB=1ok7 | SCENE= }}
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'''A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS'''
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===A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS===
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==Overview==
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Most DNA polymerases interact with their cognate processive replication factor through a small peptide, this interaction being absolutely required for their function in vivo. We have solved the crystal structure of a complex between the beta sliding clamp of Escherichia coli and the 16 residue C-terminal peptide of Pol IV (P16). The seven C-terminal residues bind to a pocket located at the surface of one beta monomer. This region was previously identified as the binding site of another beta clamp binding protein, the delta subunit of the gamma complex. We show that peptide P16 competitively prevents beta-clamp-mediated stimulation of both Pol IV and alpha subunit DNA polymerase activities, suggesting that the site of interaction of the alpha subunit with beta is identical with, or overlaps that of Pol IV. This common binding site for delta, Pol IV and alpha subunit is shown to be formed by residues that are highly conserved among many bacterial beta homologs, thus defining an evolutionarily conserved hydrophobic crevice for sliding clamp ligands and a new target for antibiotic drug design.
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(as it appears on PubMed at http://www.pubmed.gov), where 14729336 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14729336}}
==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Translesion synthesis]]
[[Category: Translesion synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:57:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:19:07 2008''

Revision as of 16:19, 27 July 2008

Image:1ok7.png

Template:STRUCTURE 1ok7

A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS

Template:ABSTRACT PUBMED 14729336

About this Structure

1OK7 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competition between replicative and translesion DNA polymerases., Burnouf DY, Olieric V, Wagner J, Fujii S, Reinbolt J, Fuchs RP, Dumas P, J Mol Biol. 2004 Jan 30;335(5):1187-97. PMID:14729336

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