1b63: Difference between revisions

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[[Image:1b63.gif|left|200px]]
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{{STRUCTURE_1b63|  PDB=1b63  |  SCENE=  }}  
{{STRUCTURE_1b63|  PDB=1b63  |  SCENE=  }}  


'''MUTL COMPLEXED WITH ADPNP'''
===MUTL COMPLEXED WITH ADPNP===




==Overview==
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The MutL DNA mismatch repair protein has recently been shown to be an ATPase and to belong to an emerging ATPase superfamily that includes DNA topoisomerase II and Hsp90. We report here the crystal structures of a 40 kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate analog, ADPnP, and with product ADP. More than 60 residues that are disordered in the apoprotein structure become ordered and contribute to both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified by subsequent release of the gamma-phosphate, releases two key loops and leads to dissociation of the LN40 dimer. Dimerization of the LN40 region is required for and is the rate-limiting step in ATP hydrolysis by MutL. The ATPase activity of MutL is stimulated by DNA and likely acts as a switch to coordinate DNA mismatch repair.
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==About this Structure==
==About this Structure==
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[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Dna mismatch repair]]
[[Category: Dna mismatch repair]]
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Revision as of 18:21, 30 June 2008

File:1b63.png

Template:STRUCTURE 1b63

MUTL COMPLEXED WITH ADPNPMUTL COMPLEXED WITH ADPNP

Template:ABSTRACT PUBMED 10199405

About this StructureAbout this Structure

1B63 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair., Ban C, Junop M, Yang W, Cell. 1999 Apr 2;97(1):85-97. PMID:10199405

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