1azo: Difference between revisions

Revision as of 12:50, 21 February 2008

DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI

OverviewOverview

MutS, MutL and MutH are the three essential proteins for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL. We have crystallized MutH in two space groups and solved the structures at 1.7 and 2.3 A resolution, respectively. The active site of MutH is located at an interface between two subdomains that pivot relative to one another, as revealed by comparison of the crystal structures, and this presumably regulates the nuclease activity. The relative motion of the two subdomains in MutH correlates with the position of a protruding C-terminal helix. This helix appears to act as a molecular lever through which MutS and MutL may communicate the detection of a DNA mismatch and activate MutH. With sequence homology to Sau3AI and structural similarity to PvuII endonuclease, MutH is clearly related to these enzymes by divergent evolution, and this suggests that type II restriction endonucleases evolved from a common ancestor.

About this StructureAbout this Structure

1AZO is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases., Ban C, Yang W, EMBO J. 1998 Mar 2;17(5):1526-34. PMID:9482749

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OCA

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 '''DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI'''<br />
 ==Overview==
-MutS, MutL and MutH are the three essential proteins for initiation of, methyl-directed DNA mismatch repair to correct mistakes made during DNA, replication in Escherichia coli. MutH cleaves a newly synthesized and, unmethylated daughter strand 5' to the sequence d(GATC) in a, hemi-methylated duplex. Activation of MutH requires the recognition of a, DNA mismatch by MutS and MutL. We have crystallized MutH in two space, groups and solved the structures at 1.7 and 2.3 A resolution, respectively. The active site of MutH is located at an interface between, two subdomains that pivot relative to one another, as revealed by, comparison of the crystal structures, and this presumably regulates the, nuclease activity. The relative motion of the two subdomains in MutH, correlates with the position of a protruding C-terminal helix. This helix, appears to act as a molecular lever through which MutS and MutL may, communicate the detection of a DNA mismatch and activate MutH. With, sequence homology to Sau3AI and structural similarity to PvuII, endonuclease, MutH is clearly related to these enzymes by divergent, evolution, and this suggests that type II restriction endonucleases, evolved from a common ancestor.
+MutS, MutL and MutH are the three essential proteins for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL. We have crystallized MutH in two space groups and solved the structures at 1.7 and 2.3 A resolution, respectively. The active site of MutH is located at an interface between two subdomains that pivot relative to one another, as revealed by comparison of the crystal structures, and this presumably regulates the nuclease activity. The relative motion of the two subdomains in MutH correlates with the position of a protruding C-terminal helix. This helix appears to act as a molecular lever through which MutS and MutL may communicate the detection of a DNA mismatch and activate MutH. With sequence homology to Sau3AI and structural similarity to PvuII endonuclease, MutH is clearly related to these enzymes by divergent evolution, and this suggests that type II restriction endonucleases evolved from a common ancestor.
 ==About this Structure==
-AZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AZO OCA].
+AZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZO OCA].
 ==Reference==
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