3KI9

Crystal structure of Staphylococcus aureus metallopeptidase (Sapep/DapE) in the Mn2+ bound form

3KI9 の概要

• エントリーDOI: 10.2210/pdb3ki9/pdb
• 関連するPDBエントリー: 3KHX 3KHZ
• 分子名称: Putative dipeptidase SACOL1801, MANGANESE (II) ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: mn+2 bound form-dipeptidase (dape), metallopeptidase, sapep, m20 peptidase, dipeptidase, hydrolase, metal-binding, metalloprotease, protease
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55544.50

構造登録者

Girish, T.S.,Gopal, B. (登録日: 2009-11-01, 公開日: 2010-07-07, 最終更新日: 2023-11-01)

主引用文献

Girish, T.S.,Gopal, B.
Crystal structure of Staphylococcus aureus metallopeptidase (Sapep) reveals large domain motions between the manganese-bound and apo-states
J.Biol.Chem., 285:29406-29415, 2010

PubMed Abstract: Proteases belonging to the M20 family are characterized by diverse substrate specificity and participate in several metabolic pathways. The Staphylococcus aureus metallopeptidase, Sapep, is a member of the aminoacylase-I/M20 protein family. This protein is a Mn(2+)-dependent dipeptidase. The crystal structure of this protein in the Mn(2+)-bound form and in the open, metal-free state suggests that large interdomain movements could potentially regulate the activity of this enzyme. We note that the extended inactive conformation is stabilized by a disulfide bond in the vicinity of the active site. Although these cysteines, Cys(155) and Cys(178), are not active site residues, the reduced form of this enzyme is substantially more active as a dipeptidase. These findings acquire further relevance given a recent observation that this enzyme is only active in methicillin-resistant S. aureus. The structural and biochemical features of this enzyme provide a template for the design of novel methicillin-resistant S. aureus-specific therapeutics.

PubMed: 20610394
DOI: 10.1074/jbc.M110.147579

実験手法

X-RAY DIFFRACTION (2.9 Å)