4qwq: Difference between revisions
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==Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus== | ==Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus== | ||
<StructureSection load='4qwq' size='340' side='right' caption='[[4qwq]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4qwq' size='340' side='right'caption='[[4qwq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qwq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QWQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QWQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qwq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QWQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QWQ 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=4qwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwq OCA], [http://pdbe.org/4qwq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qwq RCSB], [http://www.ebi.ac.uk/pdbsum/4qwq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qwq ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">saeR, CH52_02235, X998_0755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=4qwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwq OCA], [http://pdbe.org/4qwq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qwq RCSB], [http://www.ebi.ac.uk/pdbsum/4qwq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qwq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4qwq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4qwq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Response regulator|Response regulator]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Fan, X]] | [[Category: Fan, X]] | ||
[[Category: Li, X]] | [[Category: Li, X]] | ||
Revision as of 12:11, 24 April 2019
Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureusCrystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus
Structural highlights
Publication Abstract from PubMedThe SaeR/S two-component regulatory system is essential for controlling the expression of many virulence factors in Staphylococcus aureus. SaeR, a member of the OmpR/PhoB family, is a response regulator with an N-terminal regulatory domain and a C-terminal DNA-binding domain. In order to elucidate how SaeR binds to the promoter regions of target genes, the crystal structure of the DNA-binding domain of SaeR (SaeR(DBD)) was solved at 2.5 A resolution. The structure reveals that SaeR(DBD) exists as a monomer and has the canonical winged helix-turn-helix module. EMSA experiments suggested that full-length SaeR can bind to the P1 promoter and that the binding affinity is higher than that of its C-terminal DNA-binding domain. Five key residues on the winged helix-turn-helix module were verified to be important for binding to the P1 promoter in vitro and for the physiological function of SaeR in vivo. Structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus.,Fan X, Zhang X, Zhu Y, Niu L, Teng M, Sun B, Li X Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1768-76. doi:, 10.1107/S1399004715010287. Epub 2015 Jul 31. PMID:26249357[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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