1ok7
From Proteopedia
(New page: 200px<br /><applet load="1ok7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ok7, resolution 1.65Å" /> '''A CONSERVED PROTEIN ...) |
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| - | [[Image:1ok7.jpg|left|200px]]<br /><applet load="1ok7" size=" | + | [[Image:1ok7.jpg|left|200px]]<br /><applet load="1ok7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ok7, resolution 1.65Å" /> | caption="1ok7, resolution 1.65Å" /> | ||
'''A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS'''<br /> | '''A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Most DNA polymerases interact with their cognate processive replication | + | 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== | ==About this Structure== | ||
| - | 1OK7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http:// | + | 1OK7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burnouf, D | + | [[Category: Burnouf, D Y.]] |
[[Category: Dumas, P.]] | [[Category: Dumas, P.]] | ||
| - | [[Category: Fuchs, R | + | [[Category: Fuchs, R P.P.]] |
[[Category: Fujii, S.]] | [[Category: Fujii, S.]] | ||
[[Category: Olieric, V.]] | [[Category: Olieric, V.]] | ||
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[[Category: translesion synthesis]] | [[Category: translesion synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:43 2008'' |
Revision as of 12:18, 21 February 2008
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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. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 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 Thu Feb 21 14:18:43 2008
Categories: DNA-directed DNA polymerase | Escherichia coli | Protein complex | Burnouf, D Y. | Dumas, P. | Fuchs, R P.P. | Fujii, S. | Olieric, V. | Reinbolt, J. | Wagner, J. | Dna polymerase iv | Dna replication | Peptide inhibition | Sliding clamp | Transferase; dna-directed dna polymerase | Translesion synthesis
