1p4x
From Proteopedia
(New page: 200px<br /><applet load="1p4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4x, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1p4x.jpg|left|200px]]<br /><applet load="1p4x" size=" | + | [[Image:1p4x.jpg|left|200px]]<br /><applet load="1p4x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p4x, resolution 2.20Å" /> | caption="1p4x, resolution 2.20Å" /> | ||
'''Crystal structure of SarS protein from Staphylococcus Aureus'''<br /> | '''Crystal structure of SarS protein from Staphylococcus Aureus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The expression of virulence determinants in Staphylococcus aureus is | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Cheung, A | + | [[Category: Cheung, A L.]] |
[[Category: Dai, S.]] | [[Category: Dai, S.]] | ||
[[Category: Li, R.]] | [[Category: Li, R.]] | ||
| - | [[Category: Manna, A | + | [[Category: Manna, A C.]] |
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
[[Category: winged-helix protein]] | [[Category: winged-helix protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:08 2008'' |
Revision as of 12:25, 21 February 2008
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Crystal structure of SarS protein from Staphylococcus Aureus
Overview
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.
About this Structure
1P4X is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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
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