2W7S

SplA serine protease of Staphylococcus aureus (1.8A)

2W7S の概要

• エントリーDOI: 10.2210/pdb2w7s/pdb
• 関連するPDBエントリー: 2W7U
• 分子名称: SERINE PROTEASE SPLA (2 entities in total)
• 機能のキーワード: hydrolase, family s1
• 由来する生物種: STAPHYLOCOCCUS AUREUS
• 細胞内の位置: Secreted: Q2FXC2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 87541.93

構造登録者

Stec-Niemczyka, J.,Pustelny, K.,Kisielewska, M.,Bista, M.,Boulware, K.T.,Stennicke, H.R.,Thogersen, I.B.,Daugherty, P.S.,Enghild, J.J.,Popowicz, G.M.,Dubin, A.,Potempa, J.,Dubin, G. (登録日: 2008-12-30, 公開日: 2010-03-31, 最終更新日: 2023-12-13)

主引用文献

Stec-Niemczyka, J.,Pustelny, K.,Kisielewska, M.,Bista, M.,Boulware, K.T.,Stennicke, H.R.,Thogersen, I.B.,Daugherty, P.S.,Enghild, J.J.,Popowicz, G.M.,Dubin, A.,Potempa, J.,Dubin, G.
Structural and Functional Characterization of Spla, an Exclusively Specific Protease of Staphylococcus Aureus
Biochem.J., 419:555-, 2009

PubMed Abstract: 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.

PubMed: 19175361
DOI: 10.1042/BJ20081351

実験手法

X-RAY DIFFRACTION (1.8 Å)