3KL9

Crystal structure of PepA from Streptococcus pneumoniae

3KL9 の概要

• エントリーDOI: 10.2210/pdb3kl9/pdb
• 分子名称: Glutamyl aminopeptidase, ZINC ION (3 entities in total)
• 機能のキーワード: glutamyl aminopeptidase, pepa, tetrahedral aminopeptidase, substrate specificity, metallopeptidase m42, aminopeptidase, hydrolase
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 459384.62

構造登録者

Kim, K.K.,Lee, S.,Kim, D. (登録日: 2009-11-07, 公開日: 2010-02-02, 最終更新日: 2023-11-01)

主引用文献

Kim, D.,San, B.H.,Moh, S.H.,Park, H.J.,Kim, D.Y.,Lee, S.,Kim, K.K.
Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease
Biochem.Biophys.Res.Commun., 391:431-436, 2010

PubMed Abstract: Regulated cytosolic proteolysis is one of the key cellular processes ensuring proper functioning of a cell. M42 family proteases show a broad spectrum of substrate specificities, but the structural basis for such diversity of the substrate specificities is lagging behind biochemical data. Here we report the crystal structure of PepA from Streptococcus pneumoniae, a glutamyl aminopeptidase belonging to M42 family (SpPepA). We found that Arg-257 in the substrate binding pocket is strategically positioned so that Arg-257 can make electrostatic interactions with the acidic residue of a substrate at its N-terminus. Structural comparison of the substrate binding pocket of the M42 family proteases, along with the structure-based multiple sequence alignment, argues that the appropriate electrostatic interactions contribute to the selective substrate specificity of SpPepA.

PubMed: 19914209
DOI: 10.1016/j.bbrc.2009.11.075

実験手法

X-RAY DIFFRACTION (2.7 Å)