1bkn
From Proteopedia
(New page: 200px<br /><applet load="1bkn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bkn, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1bkn.gif|left|200px]]<br /><applet load="1bkn" size=" | + | [[Image:1bkn.gif|left|200px]]<br /><applet load="1bkn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bkn, resolution 2.9Å" /> | caption="1bkn, resolution 2.9Å" /> | ||
'''CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL'''<br /> | '''CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | MutL and its homologs are essential for DNA mismatch repair. Mutations in | + | 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== | ==About this Structure== | ||
| - | 1BKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1BKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: dna repair]] | [[Category: dna repair]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:17 2008'' |
Revision as of 09:56, 21 February 2008
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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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