3VVC
Crystal Structure of Capsular Polysaccharide Synthesizing Enzyme CapE , K126E, in apo form
3VVC の概要
エントリーDOI | 10.2210/pdb3vvc/pdb |
関連するPDBエントリー | 3VVB 4G5H |
分子名称 | Capsular polysaccharide synthesis enzyme Cap8E, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total) |
機能のキーワード | rossmann fold, short-chain dehydrogenase/reductase, capsular polysaccharide synthesis, oxidase, epimerase, lyase |
由来する生物種 | Staphylococcus aureus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 42180.17 |
構造登録者 | Miyafusa, T.,Caaveiro, J.M.,Tanaka, Y.,Tsumoto, K. (登録日: 2012-07-18, 公開日: 2013-06-12, 最終更新日: 2024-03-20) |
主引用文献 | Miyafusa, T.,Caaveiro, J.M.,Tanaka, Y.,Tanner, M.E.,Tsumoto, K. Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus. Biosci.Rep., 33:463-474, 2013 Cited by PubMed Abstract: 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. PubMed: 23611437DOI: 10.1042/BSR20130017 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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