5GYJ

Structure of catalytically active sortase from Clostridium difficile

5GYJ の概要

• エントリーDOI: 10.2210/pdb5gyj/pdb
• 関連するPDBエントリー: 4UX7
• 分子名称: Putative peptidase C60B, sortase B (2 entities in total)
• 機能のキーワード: transpeptidase, cys-his-arg catalytic triad, hydrolase
• 由来する生物種: Peptoclostridium difficile (strain 630)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26189.28

構造登録者

Yin, J.-C.,Fei, C.-H.,Hsiao, Y.-Y.,Nix, J.C.,Huang, I.-H.,Wang, S. (登録日: 2016-09-22, 公開日: 2017-01-04, 最終更新日: 2023-11-08)

主引用文献

Yin, J.C.,Fei, C.H.,Lo, Y.C.,Hsiao, Y.Y.,Chang, J.C.,Nix, J.C.,Chang, Y.Y.,Yang, L.W.,Huang, I.H.,Wang, S.
Structural Insights into Substrate Recognition by Clostridium difficile Sortase.
Front Cell Infect Microbiol, 6:160-160, 2016

PubMed Abstract: Sortases function as cysteine transpeptidases that catalyze the covalent attachment of virulence-associated surface proteins into the cell wall peptidoglycan in Gram-positive bacteria. The substrate proteins targeted by sortase enzymes have a cell wall sorting signal (CWSS) located at the C-terminus. Up to date, it is still not well understood how sortases with structural resemblance among different classes and diverse species of bacteria achieve substrate specificity. In this study, we focus on elucidating the molecular basis for specific recognition of peptide substrate PPKTG by sortase B (Cd-SrtB). Combining structural studies, biochemical assays and molecular dynamics simulations, we have constructed a computational model of Cd-SrtB-PPKTG complex and have validated the model by site-directed mutagensis studies and fluorescence resonance energy transfer (FRET)-based assay. Furthermore, we have revealed that the fourth amino acid in the N-terminal direction from cleavage site of PPKTG forms specific interaction with Cd-SrtB and plays an essential role in configuring the peptide to allow more efficient substrate-specific cleavage by Cd-SrtB.

PubMed: 27921010
DOI: 10.3389/fcimb.2016.00160

実験手法

X-RAY DIFFRACTION (2.801 Å)