1P4X

Crystal structure of SarS protein from Staphylococcus Aureus

Summary for 1P4X

• Entry DOI: 10.2210/pdb1p4x/pdb
• Related: 1HSJ
• Descriptor: staphylococcal accessory regulator A homologue (2 entities in total)
• Functional Keywords: winged-helix protein, transcription
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm : P0C0R2
• Total number of polymer chains: 1
• Total formula weight: 29938.89

Authors

Li, R.,Manna, A.C.,Dai, S.,Cheung, A.L.,Zhang, G. (deposition date: 2003-04-24, release date: 2003-07-08, Last modification date: 2024-02-14)

Primary citation

Li, R.,Manna, A.C.,Dai, S.,Cheung, A.L.,Zhang, G.
Crystal structure of the SarS protein from Staphylococcus aureus
J.BACTERIOL., 185:4219-4225, 2003

PubMed Abstract: 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.

PubMed: 12837797
DOI: 10.1128/JB.185.14.4219-4225.2003

Experimental method

X-RAY DIFFRACTION (2.2 Å)