1unn: Difference between revisions

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[[Image:1unn.gif|left|200px]]
{{Seed}}
[[Image:1unn.png|left|200px]]


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{{STRUCTURE_1unn|  PDB=1unn  |  SCENE=  }}  
{{STRUCTURE_1unn|  PDB=1unn  |  SCENE=  }}  


'''COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV'''
===COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV===




==Overview==
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Y-family DNA polymerases can extend primer strands across template strand lesions that stall replicative polymerases. The poor processivity and fidelity of these enzymes, key to their biological role, requires that their access to the primer-template junction is both facilitated and regulated in order to minimize mutations. These features are believed to be provided by interaction with processivity factors, beta-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases. The basis for this interaction is revealed by the crystal structure of the complex between the 'little finger' domain of the Y-family DNA polymerase Pol IV and the beta-clamp processivity factor, both from Escherichia coli. The main interaction involves a C-terminal peptide of Pol IV, and is similar to interactions seen between isolated peptides and other processivity factors. However, this first structure of an entire domain of a binding partner with an assembled clamp reveals a substantial secondary interface, which maintains the polymerase in an inactive orientation, and may regulate the switch between replicative and Y-family DNA polymerases in response to a template strand lesion.
The line below this paragraph, {{ABSTRACT_PUBMED_14592985}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14592985 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14592985}}


==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Translesion]]
[[Category: Translesion]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:28:25 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:20:50 2008''

Revision as of 12:20, 29 July 2008

File:1unn.png

Template:STRUCTURE 1unn

COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV

Template:ABSTRACT PUBMED 14592985

About this Structure

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

Reference

Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp., Bunting KA, Roe SM, Pearl LH, EMBO J. 2003 Nov 3;22(21):5883-92. PMID:14592985

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