4qwq: Difference between revisions

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 <StructureSection load='4qwq' size='340' side='right'caption='[[4qwq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[4qwq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QWQ FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501&#8491;</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwq OCA], [https://pdbe.org/4qwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qwq RCSB], [https://www.ebi.ac.uk/pdbsum/4qwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qwq ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/SAER_STAA8 SAER_STAA8] Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (Hla, Hlb), Coa, DNase, Spa and cell wall-associated proteins (Emp, Eap, FnbA). Acts probably downstream of the Agr system in the regulatory cascade of virulence factors.<ref>PMID:10436918</ref> <ref>PMID:11442841</ref> <ref>PMID:14523104</ref> <ref>PMID:14563862</ref> <ref>PMID:15941988</ref> <ref>PMID:17041853</ref> <ref>PMID:7922890</ref> <ref>PMID:8742355</ref> <ref>PMID:9211714</ref>
-The 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<ref>PMID:26249357</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4qwq" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Response regulator|Response regulator]]
+*[[Response regulator 3D structure|Response regulator 3D structure]]
 == References ==
 <references/>
@@ Line 24: / Line 17: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Fan, X]]
+[[Category: Staphylococcus aureus]]
-[[Category: Li, X]]
+[[Category: Fan X]]
-[[Category: Teng, M]]
+[[Category: Li X]]
-[[Category: Zhang, X]]
+[[Category: Teng M]]
-[[Category: Zhu, Y]]
+[[Category: Zhang X]]
-[[Category: Dna]]
+[[Category: Zhu Y]]
-[[Category: Gene expression regulation]]
-[[Category: Transcription regulator]]
-[[Category: Winged helix-turn-helix]]