4D59

Clostridial Cysteine protease Cwp84 C116A after propeptide cleavage

4D59 の概要

• エントリーDOI: 10.2210/pdb4d59/pdb
• 関連するPDBエントリー: 4D5A
• 分子名称: CELL SURFACE PROTEIN (PUTATIVE CELL SURFACE-ASSOCIATED CYSTEINE PROTEASE), CALCIUM ION, O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500), ... (4 entities in total)
• 機能のキーワード: hydrolase, s-layer, surface layer
• 由来する生物種: PEPTOCLOSTRIDIUM DIFFICILE QCD-32G58
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91473.53

構造登録者

Bradshaw, W.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R. (登録日: 2014-11-03, 公開日: 2015-03-04, 最終更新日: 2023-12-20)

主引用文献

Bradshaw, W.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R.
Cwp84, a Clostridium Difficile Cysteine Protease, Exhibits Conformational Flexibility in the Absence of its Propeptide
Acta Crystallogr.,Sect.F, 71:295-, 2015

PubMed Abstract: In recent decades, the global healthcare problems caused by Clostridium difficile have increased at an alarming rate. A greater understanding of this antibiotic-resistant bacterium, particularly with respect to how it interacts with the host, is required for the development of novel strategies for fighting C. difficile infections. The surface layer (S-layer) of C. difficile is likely to be of significant importance to host-pathogen interactions. The mature S-layer is formed by a proteinaceous array consisting of multiple copies of a high-molecular-weight and a low-molecular-weight S-layer protein. These components result from the cleavage of SlpA by Cwp84, a cysteine protease. The structure of a truncated Cwp84 active-site mutant has recently been reported and the key features have been identified, providing the first structural insights into the role of Cwp84 in the formation of the S-layer. Here, two structures of Cwp84 after propeptide cleavage are presented and the three conformational changes that are observed are discussed. These changes result in a reconfiguration of the active site and exposure of the hydrophobic pocket.

PubMed: 25760704
DOI: 10.1107/S2053230X15001065

実験手法

X-RAY DIFFRACTION (1.84 Å)