4qwq: Difference between revisions

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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]] 2.501&#8491;</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.
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==
==See Also==

Latest revision as of 11:59, 20 March 2024

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

4qwq is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.501Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5] [6] [7] [8] [9]

See Also

References

  1. ↑ Giraudo AT, Calzolari A, Cataldi AA, Bogni C, Nagel R. The sae locus of Staphylococcus aureus encodes a two-component regulatory system. FEMS Microbiol Lett. 1999 Aug 1;177(1):15-22. PMID:10436918 doi:10.1111/j.1574-6968.1999.tb13707.x
  2. ↑ Goerke C, Fluckiger U, Steinhuber A, Zimmerli W, Wolz C. Impact of the regulatory loci agr, sarA and sae of Staphylococcus aureus on the induction of alpha-toxin during device-related infection resolved by direct quantitative transcript analysis. Mol Microbiol. 2001 Jun;40(6):1439-47. PMID:11442841 doi:10.1046/j.1365-2958.2001.02494.x
  3. ↑ Novick RP, Jiang D. The staphylococcal saeRS system coordinates environmental signals with agr quorum sensing. Microbiology (Reading). 2003 Oct;149(Pt 10):2709-2717. PMID:14523104 doi:10.1099/mic.0.26575-0
  4. ↑ Steinhuber A, Goerke C, Bayer MG, Döring G, Wolz C. Molecular architecture of the regulatory Locus sae of Staphylococcus aureus and its impact on expression of virulence factors. J Bacteriol. 2003 Nov;185(21):6278-86. PMID:14563862 doi:10.1128/JB.185.21.6278-6286.2003
  5. ↑ Harraghy N, Kormanec J, Wolz C, Homerova D, Goerke C, Ohlsen K, Qazi S, Hill P, Herrmann M. sae is essential for expression of the staphylococcal adhesins Eap and Emp. Microbiology (Reading). 2005 Jun;151(Pt 6):1789-1800. PMID:15941988 doi:10.1099/mic.0.27902-0
  6. ↑ Xiong YQ, Willard J, Yeaman MR, Cheung AL, Bayer AS. Regulation of Staphylococcus aureus alpha-toxin gene (hla) expression by agr, sarA, and sae in vitro and in experimental infective endocarditis. J Infect Dis. 2006 Nov 1;194(9):1267-75. PMID:17041853 doi:10.1086/508210
  7. ↑ Giraudo AT, Raspanti CG, Calzolari A, Nagel R. Characterization of a Tn551-mutant of Staphylococcus aureus defective in the production of several exoproteins. Can J Microbiol. 1994 Aug;40(8):677-81. PMID:7922890 doi:10.1139/m94-107
  8. ↑ Giraudo AT, Rampone H, Calzolari A, Nagel R. Phenotypic characterization and virulence of a sae aureus. Can J Microbiol. 1996 Feb;42(2):120-3. PMID:8742355 doi:10.1139/m96-019
  9. ↑ Giraudo AT, Cheung AL, Nagel R. The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level. Arch Microbiol. 1997 Jul;168(1):53-8. PMID:9211714 doi:10.1007/s002030050469

4qwq, resolution 2.50Å

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