1aa3: Difference between revisions

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 ==C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE==
-<StructureSection load='1aa3' size='340' side='right'caption='[[1aa3]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1aa3' size='340' side='right'caption='[[1aa3]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1aa3]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1AA3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1aa3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=1aa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa3 OCA], [https://pdbe.org/1aa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa3 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa3 ProSAT], [https://www.topsan.org/Proteins/RSGI/1aa3 TOPSAN]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1aa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa3 OCA], [https://pdbe.org/1aa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa3 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa3 ProSAT], [https://www.topsan.org/Proteins/RSGI/1aa3 TOPSAN]</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]
+[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]]
@@ Line 18: / Line 19: @@
 </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=1aa3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== 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>
-</div>
-<div class="pdbe-citations 1aa3" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Recombinase A|Recombinase A]]
+*[[3D structures of recombinase A|3D structures of recombinase A]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Aihara, H]]
+[[Category: Aihara H]]
-[[Category: Ito, Y]]
+[[Category: Ito Y]]
-[[Category: Kurumizaka, H]]
+[[Category: Kurumizaka H]]
-[[Category: Structural genomic]]
+[[Category: Shibata T]]
-[[Category: Shibata, T]]
+[[Category: Terada T]]
-[[Category: Terada, T]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
-[[Category: Double-stranded dna binding domain]]
-[[Category: Rsgi]]