4qwq: Difference between revisions

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'''Unreleased structure'''


The entry 4qwq is ON HOLD
==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]] 2.50&Aring;' scene=''>
== 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>
</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>
== 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>


Authors: Fan, X., Zhu, Y., Zhang, X., Teng, M., Li, X.
==See Also==
 
*[[Response regulator 3D structure|Response regulator 3D structure]]
Description: Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Fan X]]
[[Category: Li X]]
[[Category: Teng M]]
[[Category: Zhang X]]
[[Category: Zhu Y]]

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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