1aa3

<StructureSection load='1aa3' size='340' side='right' caption='[[1aa3]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1aa3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AA3 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=1aa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa3 OCA], [http://pdbe.org/1aa3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aa3 RCSB], [http://www.ebi.ac.uk/pdbsum/1aa3 PDBsum], [http://www.topsan.org/Proteins/RSGI/1aa3 TOPSAN]</span></td></tr>

[[http://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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/1aa3_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

RecA protein and its homologs catalyze homologous pairing of dsDNA and ssDNA, a critical reaction in homologous genetic recombination in various organisms from a virus, microbes to higher eukaryotes. In this reaction, RecA protein forms a nucleoprotein filament on ssDNA, which in turn binds to naked dsDNA for homology search. We suggested that the C-terminal domain of RecA protein plays a role in capturing the dsDNA. Here, we isolated the C-terminal domain as a soluble form and determined the solution structure by NMR spectroscopy. The overall folding of the NMR structure agrees with that of the corresponding part of the reported crystal structure, but a remarkable difference was found in a solvent-exposed region due to intermolecular contacts in the crystal. Then, we studied the interaction between the C-terminal domain and DNA, and found that significant chemical shift changes were induced in a specific region by titration with dsDNA. SsDNA induced a much smaller chemical shift perturbation. The difference of DNA concentrations to give the half-saturation of the chemical shift change showed a higher affinity of the C-terminal region toward dsDNA. Combined with our previous results, these provide direct evidence that the defined region in the C-terminal domain furnishes a binding surface for DNA.

An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing.,Aihara H, Ito Y, Kurumizaka H, Terada T, Yokoyama S, Shibata T J Mol Biol. 1997 Nov 28;274(2):213-21. PMID:9398528<ref>PMID:9398528</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1aa3" style="background-color:#fffaf0;"></div>

*[[Recombinase A|Recombinase A]]

[[Category: Escherichia coli]]

[[Category: Aihara, H]]

[[Category: Ito, Y]]

[[Category: Kurumizaka, H]]

[[Category: Structural genomic]]

[[Category: Shibata, T]]

[[Category: Terada, T]]

[[Category: Yokoyama, S]]

[[Category: Rsgi]]