2w7s | pdb_00002w7s

SPLA SERINE PROTEASE OF STAPHYLOCOCCUS AUREUS (1.8A)

spinqualitylabelsall models 2w7s, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w7s is a 4 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2w7u Activity: Glutamyl endopeptidase, with EC number 3.4.21.19 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Staphylococcus aureus is a dangerous human pathogen whose antibiotic resistance is steadily increasing and no efficient vaccine is as yet available. This serious threat drives extensive studies on staphylococcal physiology and pathogenicity pathways, especially virulence factors. Spl (serine protease-like) proteins encoded by an operon containing up to six genes are a good example of poorly characterized secreted proteins probably involved in virulence. In the present study, we describe an efficient heterologous expression system for SplA and detailed biochemical and structural characterization of the recombinant SplA protease. The enzyme shares a significant sequence homology to V8 protease and epidermolytic toxins which are well documented staphylococcal virulence factors. SplA has a very narrow substrate specificity apparently imposed by the precise recognition of three amino acid residues positioned N-terminal to the hydrolysed peptide bond. To explain determinants of this extended specificity we resolve the crystal structure of SplA and define the consensus model of substrate binding. Furthermore we demonstrate that artificial N-terminal elongation of mature SplA mimicking a naturally present signal peptide abolishes enzymatic activity. The probable physiological role of the process is discussed. Of interest, even though precise N-terminal trimming is a common regulatory mechanism among S1 family enzymes, the crystal structure of SplA reveals novel significantly different mechanistic details. Structural and functional characterization of SplA, an exclusively specific protease of Staphylococcus aureus.,Stec-Niemczyk J, Pustelny K, Kisielewska M, Bista M, Boulware KT, Stennicke HR, Thogersen IB, Daugherty PS, Enghild JJ, Baczynski K, Popowicz GM, Dubin A, Potempa J, Dubin G Biochem J. 2009 May 1;419(3):555-64. PMID:19175361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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