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New page: left|200px<br /><applet load="2reb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2reb, resolution 2.3Å" /> '''THE STRUCTURE OF THE ...
 
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[[Image:2reb.gif|left|200px]]<br /><applet load="2reb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2reb, resolution 2.3&Aring;" />
'''THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER'''<br />


==Overview==
==THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER==
The 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.
<StructureSection load='2reb' size='340' side='right'caption='[[2reb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2reb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2REB 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]] 2.3&#8491;</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=2reb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2reb OCA], [https://pdbe.org/2reb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2reb RCSB], [https://www.ebi.ac.uk/pdbsum/2reb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2reb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECA_ECOLI 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 ==
[[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/re/2reb_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=2reb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2REB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2REB OCA].
*[[Recombinase A|Recombinase A]]
 
*[[3D structures of recombinase A|3D structures of recombinase A]]
==Reference==
__TOC__
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1731246 1731246]
</StructureSection>
[[Category: Deleted entry]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Steitz, T.A.]]
[[Category: Steitz TA]]
[[Category: Story, R.M.]]
[[Category: Story RM]]
[[Category: homologous recombination]]
[[Category: self-cleavage stimulation]]
 
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