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3kdk

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Revision as of 18:09, 25 December 2014

Structure of the C-terminal domain of Bacillus subtilis MutL bound to Zn2+

Structural highlights

3kdk is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3gab, 3kdg
Gene:	BSU17050, mutL (Bacillus subtilis)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MUTL_BACSU] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). Overexpression of mutSL partially suppresses the high spontaneous mutation frequency of a ytkD/mutM/yfhQ triple disruption which lacks the system required to prevent damage by oxidized guanine (8-oxo-dGTP). This suggests that MutSL also functions to repair mismatches due to oxidative stress in both growing and stationary phase cells.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

DNA mismatch repair corrects errors that have escaped polymerase proofreading, increasing replication fidelity 100- to 1000-fold in organisms ranging from bacteria to humans. The MutL protein plays a central role in mismatch repair by coordinating multiple protein-protein interactions that signal strand removal upon mismatch recognition by MutS. Here we report the crystal structure of the endonuclease domain of Bacillus subtilis MutL. The structure is organized in dimerization and regulatory subdomains connected by a helical lever spanning the conserved endonuclease motif. Additional conserved motifs cluster around the lever and define a Zn(2+)-binding site that is critical for MutL function in vivo. The structure unveils a powerful inhibitory mechanism to prevent undesired nicking of newly replicated DNA and allows us to propose a model describing how the interaction with MutS and the processivity clamp could license the endonuclease activity of MutL. The structure also provides a molecular framework to propose and test additional roles of MutL in mismatch repair.

Structure of the endonuclease domain of MutL: unlicensed to cut.,Pillon MC, Lorenowicz JJ, Uckelmann M, Klocko AD, Mitchell RR, Chung YS, Modrich P, Walker GC, Simmons LA, Friedhoff P, Guarne A Mol Cell. 2010 Jul 9;39(1):145-51. PMID:20603082^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vidales LE, Cardenas LC, Robleto E, Yasbin RE, Pedraza-Reyes M. Defects in the error prevention oxidized guanine system potentiate stationary-phase mutagenesis in Bacillus subtilis. J Bacteriol. 2009 Jan;191(2):506-13. doi: 10.1128/JB.01210-08. Epub 2008 Nov 14. PMID:19011023 doi:http://dx.doi.org/10.1128/JB.01210-08
↑ Pillon MC, Lorenowicz JJ, Uckelmann M, Klocko AD, Mitchell RR, Chung YS, Modrich P, Walker GC, Simmons LA, Friedhoff P, Guarne A. Structure of the endonuclease domain of MutL: unlicensed to cut. Mol Cell. 2010 Jul 9;39(1):145-51. PMID:20603082 doi:10.1016/j.molcel.2010.06.027

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kdk"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kdk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kdk RCSB], [http://www.ebi.ac.uk/pdbsum/3kdk PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MUTL_BACSU MUTL_BACSU]] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). Overexpression of mutSL partially suppresses the high spontaneous mutation frequency of a ytkD/mutM/yfhQ triple disruption which lacks the system required to prevent damage by oxidized guanine (8-oxo-dGTP). This suggests that MutSL also functions to repair mismatches due to oxidative stress in both growing and stationary phase cells.<ref>PMID:19011023</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3kdk

From Proteopedia

Revision as of 18:09, 25 December 2014

Structure of the C-terminal domain of Bacillus subtilis MutL bound to Zn2+

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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