1p4x

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(New page: 200px<br /><applet load="1p4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4x, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:1p4x.jpg|left|200px]]<br /><applet load="1p4x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p4x, resolution 2.20&Aring;" />
 
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'''Crystal structure of SarS protein from Staphylococcus Aureus'''<br />
 
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==Overview==
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==Crystal structure of SarS protein from Staphylococcus Aureus==
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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.
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<StructureSection load='1p4x' size='340' side='right'caption='[[1p4x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1P4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P4X OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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==Reference==
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</table>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837797 12837797]
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== Function ==
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[[Category: Single protein]]
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[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Cheung, A.L.]]
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[[Category: Cheung AL]]
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[[Category: Dai, S.]]
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[[Category: Dai S]]
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[[Category: Li, R.]]
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[[Category: Li R]]
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[[Category: Manna, A.C.]]
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[[Category: Manna AC]]
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[[Category: Zhang, G.]]
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[[Category: Zhang G]]
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[[Category: winged-helix protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:28:41 2007''
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Current revision

Crystal structure of SarS protein from Staphylococcus Aureus

PDB ID 1p4x

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