5jrj
From Proteopedia
(Difference between revisions)
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<StructureSection load='5jrj' size='340' side='right' caption='[[5jrj]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5jrj' size='340' side='right' caption='[[5jrj]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jrj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JRJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JRJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jrj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35892 Atcc 35892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JRJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JRJ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">recA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=964 ATCC 35892])</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=5jrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jrj OCA], [http://pdbe.org/5jrj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jrj RCSB], [http://www.ebi.ac.uk/pdbsum/5jrj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jrj ProSAT]</span></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=5jrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jrj OCA], [http://pdbe.org/5jrj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jrj RCSB], [http://www.ebi.ac.uk/pdbsum/5jrj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jrj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bacterial RecA protein plays a role in the complex system of DNA damage repair. Here, we report the functional and structural characterization of the Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more efficient at displacing SSB protein from ssDNA than Escherichia coli RecA protein. HsRecA also promotes DNA strand exchange more efficiently. The three dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 A resolution. HsRecA protein contains a small N-terminal domain, a central core ATPase domain and a large C-terminal domain, that are similar to homologous bacterial RecA proteins. Comparative structural analysis showed that the N-terminal polymerization motif of archaeal and eukaryotic RecA family proteins are also present in bacterial RecAs. Reconstruction of electrostatic potential from the hexameric structure of HsRecA-ADP/ATP revealed a high positive charge along the inner side, where ssDNA is bound inside the filament. The properties of this surface may explain the greater capacity of HsRecA protein to bind ssDNA, forming a contiguous nucleoprotein filament, displace SSB and promote DNA exchange relative to EcRecA. Our functional and structural analyses provide insight into the molecular mechanisms of polymerization of bacterial RecA as a helical nucleoprotein filament. | ||
| + | |||
| + | Structural and Functional Studies of H. seropedicae RecA Protein - Insights into the Polymerization of RecA Protein as Nucleoprotein Filament.,Leite WC, Galvao CW, Saab SC, Iulek J, Etto RM, Steffens MB, Chitteni-Pattu S, Stanage T, Keck JL, Cox MM PLoS One. 2016 Jul 22;11(7):e0159871. doi: 10.1371/journal.pone.0159871., eCollection 2016. PMID:27447485<ref>PMID:27447485</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jrj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 35892]] | ||
[[Category: Chitteni-Pattu, S]] | [[Category: Chitteni-Pattu, S]] | ||
[[Category: Cox, M M]] | [[Category: Cox, M M]] | ||
Revision as of 05:48, 25 April 2018
Crystal Structure of Herbaspirillum seropedicae RecA
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