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6F92

Structure of the family GH92 alpha-mannosidase BT3965 from Bacteroides thetaiotaomicron in complex with Mannoimidazole (ManI)

6F92 の概要
エントリーDOI10.2210/pdb6f92/pdb
分子名称Putative alpha-1,2-mannosidase, SODIUM ION, CALCIUM ION, ... (8 entities in total)
機能のキーワードglycan, carbohydrate, glycosidase, substrate specificity, glycoside hydrolase, alpha-mannosidase, gh92, gut bacteria, microbiota, cazy, cazypedia, hydrolase
由来する生物種Bacteroides thetaiotaomicron
タンパク質・核酸の鎖数4
化学式量合計351831.70
構造登録者
Thompson, A.J.,Spears, R.J.,Zhu, Y.,Suits, M.D.L.,Williams, S.J.,Gilbert, H.J.,Davies, G.J. (登録日: 2017-12-13, 公開日: 2018-05-02, 最終更新日: 2024-01-17)
主引用文献Thompson, A.J.,Spears, R.J.,Zhu, Y.,Suits, M.D.L.,Williams, S.J.,Gilbert, H.J.,Davies, G.J.
Bacteroides thetaiotaomicron generates diverse alpha-mannosidase activities through subtle evolution of a distal substrate-binding motif.
Acta Crystallogr D Struct Biol, 74:394-404, 2018
Cited by
PubMed Abstract: A dominant human gut microbe, the well studied symbiont Bacteroides thetaiotaomicron (Bt), is a glyco-specialist that harbors a large repertoire of genes devoted to carbohydrate processing. Despite strong similarities among them, many of the encoded enzymes have evolved distinct substrate specificities, and through the clustering of cognate genes within operons termed polysaccharide-utilization loci (PULs) enable the fulfilment of complex biological roles. Structural analyses of two glycoside hydrolase family 92 α-mannosidases, BT3130 and BT3965, together with mechanistically relevant complexes at 1.8-2.5 Å resolution reveal conservation of the global enzyme fold and core catalytic apparatus despite different linkage specificities. Structure comparison shows that Bt differentiates the activity of these enzymes through evolution of a highly variable substrate-binding region immediately adjacent to the active site. These observations unveil a genetic/biochemical mechanism through which polysaccharide-processing bacteria can evolve new and specific biochemical activities from otherwise highly similar gene products.
PubMed: 29717710
DOI: 10.1107/S2059798318002942
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 6f92
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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