1bkn

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|ACTIVITY=
|ACTIVITY=
|GENE= MUTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= MUTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkn OCA], [http://www.ebi.ac.uk/pdbsum/1bkn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bkn RCSB]</span>
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[[Category: dna repair]]
[[Category: dna repair]]
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Revision as of 16:03, 30 March 2008


PDB ID 1bkn

Drag the structure with the mouse to rotate
, resolution 2.9Å
Gene: MUTL (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL


Overview

MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.

About this Structure

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

Reference

Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis., Ban C, Yang W, Cell. 1998 Nov 13;95(4):541-52. PMID:9827806

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