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1p4x

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Revision as of 11:47, 14 June 2023

Crystal structure of SarS protein from Staphylococcus Aureus

Structural highlights

1p4x is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SARS_STAA8 Transcriptional regulator that controls expression of some virulence factors in a cell density-dependent manner. Acts as an activator of the gene encoding protein A (spa). Negatively regulates the expression of alpha-hemolysin (hla).^[1] ^[2]

Publication Abstract from PubMed

The expression of virulence determinants in Staphylococcus aureus is controlled by global regulatory loci (e.g., sarA and agr). One of these determinants, protein A (spa), is activated by sarS, which encodes a 250-residue DNA-binding protein. Genetic analysis indicated that the agr locus likely mediates spa repression by suppressing the transcription of sarS. Contrary to SarA and SarR, which require homodimer formation for proper function, SarS is unusual within the SarA protein family in that it contains two homologous halves, with each half sharing sequence similarity to SarA and SarR. Here we report the 2.2 A resolution X-ray crystal structure of the SarS protein. SarS has folds similar to those of SarR and, quite plausibly, the native SarA structure. Two typical winged-helix DNA-binding domains are connected by a well-ordered loop. The interactions between the two domains are extensive and conserved. The putative DNA-binding surface is highly positively charged. In contrast, negatively charged patches are located opposite to the DNA-binding surface. Furthermore, sequence alignment and structural comparison revealed that MarR has folds similar to those of SarR and SarS. Members of the MarR protein family have previously been implicated in the negative regulation of an efflux pump involved in multiple antibiotic resistance in many gram-negative species. We propose that MarR also belongs to the winged-helix protein family and has a similar mode of DNA binding as SarR and SarS and possibly the entire SarA protein family member. Based on the structural differences of SarR, SarS, and MarR, we further classified these winged-helix proteins to three subfamilies, SarA, SarS, and MarR. Finally, a possible transcription regulation mechanism is proposed.

Crystal structure of the SarS protein from Staphylococcus aureus.,Li R, Manna AC, Dai S, Cheung AL, Zhang G J Bacteriol. 2003 Jul;185(14):4219-25. PMID:12837797^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tegmark K, Karlsson A, Arvidson S. Identification and characterization of SarH1, a new global regulator of virulence gene expression in Staphylococcus aureus. Mol Microbiol. 2000 Jul;37(2):398-409. PMID:10931334 doi:10.1046/j.1365-2958.2000.02003.x
↑ Cheung AL, Schmidt K, Bateman B, Manna AC. SarS, a SarA homolog repressible by agr, is an activator of protein A synthesis in Staphylococcus aureus. Infect Immun. 2001 Apr;69(4):2448-55. PMID:11254606 doi:10.1128/IAI.69.4.2448-2455.2001
↑ Li R, Manna AC, Dai S, Cheung AL, Zhang G. Crystal structure of the SarS protein from Staphylococcus aureus. J Bacteriol. 2003 Jul;185(14):4219-25. PMID:12837797

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p4x"

@@ Line 3: / Line 3: @@
 <StructureSection load='1p4x' size='340' side='right'caption='[[1p4x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1p4x]] is a 1 chain structure with sequence from [https://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=1P4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P4X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1p4x]] is a 1 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=1P4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P4X FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hsj|1hsj]]</div></td></tr>
+</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=1p4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4x OCA], [https://pdbe.org/1p4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p4x RCSB], [https://www.ebi.ac.uk/pdbsum/1p4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4x 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=1p4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4x OCA], [https://pdbe.org/1p4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p4x RCSB], [https://www.ebi.ac.uk/pdbsum/1p4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SARS_STAA1 SARS_STAA1]] Transcriptional regulator that controls expression of some virulence factors in a cell density-dependent manner (By similarity).
+[https://www.uniprot.org/uniprot/SARS_STAA8 SARS_STAA8] Transcriptional regulator that controls expression of some virulence factors in a cell density-dependent manner. Acts as an activator of the gene encoding protein A (spa). Negatively regulates the expression of alpha-hemolysin (hla).<ref>PMID:10931334</ref> <ref>PMID:11254606</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Cheung, A L]]
+[[Category: Staphylococcus aureus]]
-[[Category: Dai, S]]
+[[Category: Cheung AL]]
-[[Category: Li, R]]
+[[Category: Dai S]]
-[[Category: Manna, A C]]
+[[Category: Li R]]
-[[Category: Zhang, G]]
+[[Category: Manna AC]]
-[[Category: Transcription]]
+[[Category: Zhang G]]
-[[Category: Winged-helix protein]]

1p4x

From Proteopedia

Revision as of 11:47, 14 June 2023

Crystal structure of SarS protein from Staphylococcus Aureus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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