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| | <StructureSection load='1ubc' size='340' side='right'caption='[[1ubc]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='1ubc' size='340' side='right'caption='[[1ubc]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ubc]] 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=1UBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UBC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ubc]] is a 1 chain structure with sequence from [https://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=1UBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UBC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g18|1g18]], [[1g19|1g19]], [[1mo3|1mo3]], [[1mo4|1mo4]], [[1mo5|1mo5]], [[1mo6|1mo6]], [[1ube|1ube]], [[1ubf|1ubf]], [[1ubg|1ubg]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g18|1g18]], [[1g19|1g19]], [[1mo3|1mo3]], [[1mo4|1mo4]], [[1mo5|1mo5]], [[1mo6|1mo6]], [[1ube|1ube]], [[1ubf|1ubf]], [[1ubg|1ubg]]</div></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=1ubc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ubc OCA], [http://pdbe.org/1ubc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ubc RCSB], [http://www.ebi.ac.uk/pdbsum/1ubc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ubc ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ubc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ubc OCA], [https://pdbe.org/1ubc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ubc RCSB], [https://www.ebi.ac.uk/pdbsum/1ubc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ubc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [[https://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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
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.
See Also
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
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