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==Structure of Reca Protein== | |||
<StructureSection load='1ubc' size='340' side='right'caption='[[1ubc]], [[Resolution|resolution]] 3.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ubc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</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> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
== | Check<jmol> | ||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ub/1ubc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ubc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | 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<ref>PMID:12837805</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ubc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of recombinase A|3D structures of recombinase A]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis]] | |||
[[Category: Chandra NR]] | |||
[[Category: Datta S]] | |||
[[Category: Ganesh N]] | |||
[[Category: Krishna R]] | |||
[[Category: Muniyappa K]] | |||
[[Category: Vijayan M]] | |||
Latest revision as of 10:31, 25 October 2023
Structure of Reca ProteinStructure of Reca Protein
Structural highlights
FunctionRECA_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 PubMedThe 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 AlsoReferences
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