Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus

Takamitsu Miyafusa, Jose M.M. Caaveiro, Yoshikazu Tanaka, Martin E. Tanner, Kouhei Tsumoto

研究成果: Contribution to journalArticle査読

15 被引用数 (Scopus)

抄録

Enzymes synthesizing the bacterial CP (capsular polysaccharide) are attractive antimicrobial targets. However, we lack critical information about the structure and mechanism of many of them. In an effort to reduce that gap, we have determined three different crystal structures of the enzyme CapE of the human pathogen Staphylococcus aureus. The structure reveals that CapE is a member of the SDR (short-chain dehydrogenase/reductase) super-family of proteins. CapE assembles in a hexameric complex stabilized by three major contact surfaces between protein subunits. Turnover of substrate and/or coenzyme induces major conformational changes at the contact interface between protein subunits, and a displacement of the substrate-binding domain with respect to the Rossmann domain. A novel dynamic element that we called the latch is essential for remodelling of the protein-protein interface. Structural and primary sequence alignment identifies a group of SDR proteins involved in polysaccharide synthesis that share the two salient features of CapE: the mobile loop (latch) and a distinctive catalytic site (MxxxK). The relevance of these structural elements was evaluated by site-directed mutagenesis.

本文言語英語
論文番号e00043
ページ(範囲)463-474
ページ数12
ジャーナルBioscience reports
33
3
DOI
出版ステータス出版済み - 2013
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

フィンガープリント

「Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル