Crystal Structure Staphylococcus aureus ESSB cytoplasmic fragmentCrystal Structure Staphylococcus aureus ESSB cytoplasmic fragment

Structural highlights

4ann is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.05Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESSB_STAA8 Component of the type VII secretion system (Ess) (Probable). Required for the secretion of EsxA and EsxB (By similarity).[UniProtKB:P0C053]

Publication Abstract from PubMed

The type VII protein translocation/secretion system, unique to Gram-positive bacteria is a key virulence determinant in Staphylococcus aureus. We aim to characterise the architecture of this secretion machinery and now describe a study of S. aureus EssB, a 52-kDa bitopic membrane protein essential for secretion of the ESAT-6-family-proteins, the prototypic substrate of Type VII secretion. Full-length EssB was heterologously expressed in Escherichia coli, solubilised from the bacterial membrane, purified to homogeneity and shown to be dimeric. A C-terminal truncation, EssBC, and two soluble fragments termed EssB-N and EssB-C, predicted to occur on either side of the cytoplasmic membrane, have been successfully purified in recombinant form, characterised and together with the full-length protein used in crystallisation trials. EssB-N, the 25 kDa N-terminal cytoplasmic fragment, gave well-ordered crystals and we report the structure, determined by single-wavelength anomalous diffraction (SAD) targeting an SeMet derivative, refined to atomic (1.05 A) resolution. EssB-N is dimeric in solution but crystallises as a monomer and displays a fold composed of two globular domains separated by a cleft. The structure is related to that of Ser/Thr protein kinases and our study identifies that the type VII secretion system exploits and re-uses a stable modular entity and fold that has evolved to participate in protein-protein interactions in a similar fashion to the catalytically inert pseudokinases.

Characterisation of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system; atomic resolution crystal structure of the cytoplasmic segment.,Zoltner M, Fyfe PK, Palmer T, Hunter WN Biochem J. 2012 Oct 25. PMID:23098276[1]

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

References

  1. Zoltner M, Fyfe PK, Palmer T, Hunter WN. Characterisation of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system; atomic resolution crystal structure of the cytoplasmic segment. Biochem J. 2012 Oct 25. PMID:23098276 doi:http://dx.doi.org/10.1042/BJ20121209

4ann, resolution 1.05Å

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