1ok7

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[[Image:1ok7.jpg|left|200px]]
[[Image:1ok7.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ok7 |SIZE=350|CAPTION= <scene name='initialview01'>1ok7</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1ok7", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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{{STRUCTURE_1ok7| PDB=1ok7 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok7 OCA], [http://www.ebi.ac.uk/pdbsum/1ok7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ok7 RCSB]</span>
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'''A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS'''
'''A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS'''
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[[Category: Reinbolt, J.]]
[[Category: Reinbolt, J.]]
[[Category: Wagner, J.]]
[[Category: Wagner, J.]]
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[[Category: dna polymerase iv]]
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[[Category: Dna polymerase iv]]
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[[Category: dna-directed dna polymerase,dna replication]]
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[[Category: Dna-directed dna polymerase,dna replication]]
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[[Category: peptide inhibition]]
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[[Category: Peptide inhibition]]
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[[Category: sliding clamp]]
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[[Category: Sliding clamp]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: translesion synthesis]]
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[[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 Mar 30 22:46:32 2008''
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Revision as of 00:57, 3 May 2008

Image:1ok7.jpg

Template:STRUCTURE 1ok7

A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS


Overview

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.

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 Page seeded by OCA on Sat May 3 03:57:24 2008

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