2reb: Difference between revisions
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==THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER== | ==THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER== | ||
<StructureSection load='2reb' size='340' side='right' caption='[[2reb]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2reb' size='340' side='right' caption='[[2reb]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2reb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2reb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REB 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=2reb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2reb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2reb RCSB], [http://www.ebi.ac.uk/pdbsum/2reb 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=2reb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2reb OCA], [http://pdbe.org/2reb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2reb RCSB], [http://www.ebi.ac.uk/pdbsum/2reb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2reb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2reb ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2reb" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Steitz, T A]] | [[Category: Steitz, T A]] | ||
[[Category: Story, R M]] | [[Category: Story, R M]] | ||
Revision as of 05:29, 5 August 2016
THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMERTHE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER
Structural highlights
Function[RECA_ECOLI] 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. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268] 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 structure of the recA protein from Escherichia coli at 2.3-A resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 6(1) helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo. The structure of the E. coli recA protein monomer and polymer.,Story RM, Weber IT, Steitz TA Nature. 1992 Jan 23;355(6358):318-25. PMID:1731246[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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