1ubg

From Proteopedia

(Difference between revisions)

Revision as of 05:26, 11 September 2015

MsREcA-dATP complex

Structural highlights

1ubg is a 1 chain structure with sequence from "bacillus_smegmatis"_trevisan_1889 "bacillus smegmatis" trevisan 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1g19, 1mo3, 1ubc, 1ube, 1ubf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[RECA_MYCS2] Required for homologous recombination (HR) and the bypass of mutagenic DNA lesions (double strand breaks, DSB) by the SOS response. Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. Numerous X-ray crystals have been resolved under different conditions which indicate the flexibility of the protein, essential to its function. Gln-196 contributes to this plasticity by acting as a switch residue, which transmits the effect of nucleotide binding to the DNA-binding region.^[1] ^[2] ^[3]

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

The crystal structures of Mycobacterium smegmatis RecA (RecA(Ms)) and its complexes with ADP, ATPgammaS, and dATP show that RecA(Ms) has an expanded binding site like that in Mycobacterium tuberculosis RecA, although there are small differences between the proteins in their modes of nucleotide binding. Nucleotide binding is invariably accompanied by the movement of Gln 196, which appears to provide the trigger for transmitting the effect of nucleotide binding to the DNA-binding loops. These observations provide a framework for exploring the known properties of the RecA proteins.

Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes.,Datta S, Krishna R, Ganesh N, Chandra NR, Muniyappa K, Vijayan M J Bacteriol. 2003 Jul;185(14):4280-4. PMID:12837805^[4]

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

References

↑ Pitcher RS, Green AJ, Brzostek A, Korycka-Machala M, Dziadek J, Doherty AJ. NHEJ protects mycobacteria in stationary phase against the harmful effects of desiccation. DNA Repair (Amst). 2007 Sep 1;6(9):1271-6. Epub 2007 Mar 13. PMID:17360246 doi:http://dx.doi.org/10.1016/j.dnarep.2007.02.009
↑ Stephanou NC, Gao F, Bongiorno P, Ehrt S, Schnappinger D, Shuman S, Glickman MS. Mycobacterial nonhomologous end joining mediates mutagenic repair of chromosomal double-strand DNA breaks. J Bacteriol. 2007 Jul;189(14):5237-46. Epub 2007 May 11. PMID:17496093 doi:http://dx.doi.org/10.1128/JB.00332-07
↑ Gupta R, Barkan D, Redelman-Sidi G, Shuman S, Glickman MS. Mycobacteria exploit three genetically distinct DNA double-strand break repair pathways. Mol Microbiol. 2011 Jan;79(2):316-30. doi: 10.1111/j.1365-2958.2010.07463.x. Epub, 2010 Nov 24. PMID:21219454 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07463.x
↑ Datta S, Krishna R, Ganesh N, Chandra NR, Muniyappa K, Vijayan M. Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes. J Bacteriol. 2003 Jul;185(14):4280-4. PMID:12837805

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ubg"

@@ Line 2: / Line 2: @@
 <StructureSection load='1ubg' size='340' side='right' caption='[[1ubg]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ubg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UBG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ubg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_smegmatis"_trevisan_1889 "bacillus smegmatis" trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UBG FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g19|1g19]], [[1mo3|1mo3]], [[1ubc|1ubc]], [[1ube|1ube]], [[1ubf|1ubf]]</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=1ubg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ubg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ubg RCSB], [http://www.ebi.ac.uk/pdbsum/1ubg PDBsum]</span></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=1ubg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ubg OCA], [http://pdbe.org/1ubg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ubg RCSB], [http://www.ebi.ac.uk/pdbsum/1ubg PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RECA_MYCS2 RECA_MYCS2]] Required for homologous recombination (HR) and the bypass of mutagenic DNA lesions (double strand breaks, DSB) by the SOS response. Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. Numerous X-ray crystals have been resolved under different conditions which indicate the flexibility of the protein, essential to its function. Gln-196 contributes to this plasticity by acting as a switch residue, which transmits the effect of nucleotide binding to the DNA-binding region.<ref>PMID:17360246</ref> <ref>PMID:17496093</ref> <ref>PMID:21219454</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ubg" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium smegmatis]]
+[[Category: Bacillus smegmatis trevisan 1889]]
 [[Category: Chandra, N R]]
 [[Category: Datta, S]]

1ubg

From Proteopedia

Revision as of 05:26, 11 September 2015

MsREcA-dATP complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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