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4od6

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Revision as of 07:42, 5 August 2016

Structure of Smr domain of MutS2 from Deinococcus radiodurans, Mn2+ soaked

Structural highlights

4od6 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q9RSZ3_DEIRA] Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity (By similarity).[HAMAP-Rule:MF_00092][SAAS:SAAS002625_004_016263]

Publication Abstract from PubMed

The MutS2 homologues have been found widespread in most prokaryotes, which are involved in DNA repair and reactive oxygen species detoxification. The C-terminal small mutS-related (Smr) domain is critical for its endonucleolytic activity. However, the detailed catalytic mechanism is still unclear. In this study, we first investigated the in vivo role of drMutS2 in Deinococcus radiodurans, the most radiation-resistant organism exhibits the remarkable DNA repair capacity. mutS2 and recA mutS2 double knockout mutants were constructed because the phenotype was strongly masked by the predominant homologous recombination DNA repair pathway in this bacterium. Compared with the recA mutant, cells devoid of both genes showed increased sensitivity to ionizing radiation and oxidative agents, suggesting that drMutS2 is involved in RecA-independent mechanisms that enhance cellular resistance to oxidative stress-induced DNA damage. Moreover, the basal level of reductase activity and thiamine biosynthesis was induced in the absence of mutS2. To characterize its catalytic residues, the Smr domain was crystallized and soaked in buffer containing manganese ions. In contrast to native crystals, the space group of manganese-derivative crystals transformed from monoclinic to orthorhombic unexpectedly. This type of crystals showed improved diffraction resolution to 1.2A, which has the highest resolution of currently known Smr structures. Structural comparison revealed that three acidic amino-acid residues, which are all located in the alpha1 helix, changed the rotamer states after metal soaking. Mutational analysis of conserved residue glutamic acid 710 to alanine yielded a drMutS2 variant with impaired nuclease activity, and could only partially rescue the radiosensitive phenotype of the mutS2 null strain, indicating that glutamic acid 710 is the catalytic residue.

Structural and functional studies of MutS2 from Deinococcus radiodurans.,Zhang H, Xu Q, Lu M, Xu X, Wang Y, Wang L, Zhao Y, Hua Y DNA Repair (Amst). 2014 May 5. pii: S1568-7864(14)00125-6. doi:, 10.1016/j.dnarep.2014.04.012. PMID:24811920^[1]

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

References

↑ Zhang H, Xu Q, Lu M, Xu X, Wang Y, Wang L, Zhao Y, Hua Y. Structural and functional studies of MutS2 from Deinococcus radiodurans. DNA Repair (Amst). 2014 May 5. pii: S1568-7864(14)00125-6. doi:, 10.1016/j.dnarep.2014.04.012. PMID:24811920 doi:http://dx.doi.org/10.1016/j.dnarep.2014.04.012

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4od6"

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 ==Structure of Smr domain of MutS2 from Deinococcus radiodurans, Mn2+ soaked==
 <StructureSection load='4od6' size='340' side='right' caption='[[4od6]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4od6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OD6 FirstGlance]. <br>
-</td></tr><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=4od6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4od6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4od6 RCSB], [http://www.ebi.ac.uk/pdbsum/4od6 PDBsum]</span></td></tr>
+</td></tr><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=4od6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4od6 OCA], [http://pdbe.org/4od6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4od6 RCSB], [http://www.ebi.ac.uk/pdbsum/4od6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4od6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4od6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4od6

From Proteopedia

Revision as of 07:42, 5 August 2016

Structure of Smr domain of MutS2 from Deinococcus radiodurans, Mn2+ soaked

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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