2WV7

Intracellular subtilisin precursor from B. clausii

2WV7 の概要

• エントリーDOI: 10.2210/pdb2wv7/pdb
• 関連するPDBエントリー: 2WWT
• 分子名称: INTRACELLULAR SUBTILISIN PROTEASE, SODIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, intracellular proteinase regulation
• 由来する生物種: BACILLUS CLAUSII
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 209779.07

構造登録者

Vevodova, J.,Gamble, M.,Ariza, A.,Dodson, E.,Jones, D.D.,Wilson, K.S. (登録日: 2009-10-15, 公開日: 2010-09-08, 最終更新日: 2023-12-20)

主引用文献

Vevodova, J.,Gamble, M.,Kunze, G.,Ariza, A.,Dodson, E.,Jones, D.D.,Wilson, K.S.
Crystal Structure of an Intracellular Subtilisin Reveals Novel Structural Features Unique to This Subtilisin Family.
Structure, 18:744-, 2010

PubMed Abstract: The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other subtilisins, ISP from B. clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues.

PubMed: 20541512
DOI: 10.1016/J.STR.2010.03.008

実験手法

X-RAY DIFFRACTION (2.45 Å)