4UX7

Structure of a Clostridium difficile sortase

4UX7 の概要

• エントリーDOI: 10.2210/pdb4ux7/pdb
• 分子名称: PUTATIVE PEPTIDASE C60B, SORTASE B, DI(HYDROXYETHYL)ETHER, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: hydrolase, sortase
• 由来する生物種: CLOSTRIDIUM DIFFICILE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57436.23

構造登録者

Chambers, C.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R. (登録日: 2014-08-19, 公開日: 2015-04-01, 最終更新日: 2024-01-10)

主引用文献

Chambers, C.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R.
Structure and Function of a Clostridium Difficile Sortase Enzyme.
Sci.Rep., 5:9449-, 2015

PubMed Abstract: Sortase enzymes are responsible for covalent anchoring of specific proteins to the peptidoglycan of the cell wall of gram-positive bacteria. In some gram-positive bacteria (e.g. Staphylococcus aureus), sortases have been found to be essential for pathogenesis and their inhibitors are under development as potential novel therapeutics. Here we provide the first report on the structural characterisation of the C. difficile sortase. An active site mutant was crystallised and its structure determined to 2.55 Å by X-ray diffraction to provide structural insight into its catalytic mechanism. In order to elucidate the role of the sortase in the cell wall biogenesis, a C. difficile sortase knockout strain was constructed by intron mutagenesis. Characterisation of this mutant led to the discovery that the putative adhesin CD0386 is anchored to the peptidoglycan of C. difficile by the sortase SrtB and that an SPKTG peptide motif is involved in the transpeptidation reaction with the C. difficile peptidoglycan. In an animal model for C. difficile infection, the SrtB mutant caused disease at a similar rate of onset as the wild type strain. In conclusion, our detailed study shows that the SrtB enzyme from C. difficile does not play an essential role in pathogenesis.

PubMed: 25801974
DOI: 10.1038/SREP09449

実験手法

X-RAY DIFFRACTION (2.55 Å)