1ubc: Difference between revisions

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{{Seed}}
[[Image:1ubc.png|left|200px]]


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==Structure of Reca Protein==
The line below this paragraph, containing "STRUCTURE_1ubc", creates the "Structure Box" on the page.
<StructureSection load='1ubc' size='340' side='right'caption='[[1ubc]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<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>
{{STRUCTURE_1ubc|  PDB=1ubc  |  SCENE= }}
</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.


===Structure of Reca Protein===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ubc" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12837805}}, adds the Publication Abstract to the page
*[[3D structures of recombinase A|3D structures of recombinase A]]
(as it appears on PubMed at http://www.pubmed.gov), where 12837805 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12837805}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1UBC is a 1 chain structure of 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=1UBC OCA].
[[Category: Mycolicibacterium smegmatis]]
 
[[Category: Chandra NR]]
==Reference==
[[Category: Datta S]]
<ref group="xtra">PMID:12837805</ref><references group="xtra"/>
[[Category: Ganesh N]]
[[Category: Mycobacterium smegmatis]]
[[Category: Krishna R]]
[[Category: Chandra, N R.]]
[[Category: Muniyappa K]]
[[Category: Datta, S.]]
[[Category: Vijayan M]]
[[Category: Ganesh, N.]]
[[Category: Krishna, R.]]
[[Category: Muniyappa, K.]]
[[Category: Vijayan, M.]]
[[Category: Dna-repair]]
[[Category: Recombination]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:58:28 2009''

Latest revision as of 10:31, 25 October 2023

Structure of Reca ProteinStructure of Reca Protein

Structural highlights

1ubc is a 1 chain structure with sequence from Mycolicibacterium smegmatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

1ubc, resolution 3.80Å

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