4qwq
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501Å</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> | </table> | ||
== Function == | == Function == | ||
[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> | [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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4qwq" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus
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Categories: Large Structures | Staphylococcus aureus | Fan X | Li X | Teng M | Zhang X | Zhu Y
