6BS6
SusG with mixed linkage amylosaccharide
6BS6 の概要
| エントリーDOI | 10.2210/pdb6bs6/pdb |
| 関連するBIRD辞書のPRD_ID | PRD_900009 PRD_900010 |
| 分子名称 | Alpha-amylase SusG, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (10 entities in total) |
| 機能のキーワード | glycoside hydrolase family 13, gh13, amylase, susg, hydrolase |
| 由来する生物種 | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 156343.92 |
| 構造登録者 | |
| 主引用文献 | Arnal, G.,Cockburn, D.W.,Brumer, H.,Koropatkin, N.M. Structural basis for the flexible recognition of alpha-glucan substrates by Bacteroides thetaiotaomicron SusG. Protein Sci., 27:1093-1101, 2018 Cited by PubMed Abstract: Bacteria that reside in the mammalian intestinal tract efficiently hydrolyze dietary carbohydrates, including starch, that escape digestion in the small intestine. Starch is an abundant dietary carbohydrate comprised of α1,4 and α1,6 linked glucose, yet mammalian intestinal glucoamylases cannot effectively hydrolyze starch that has frequent α1,6 branching as these structures hinder recognition and processing by α1,4-specific amylases. Here we present the structure of the cell surface amylase SusG from Bacteroides thetaiotaomicron complexed with a mixed linkage amylosaccharide generated from transglycosylation during crystallization. Although SusG is specific for α1,4 glucosidic bonds, binding of this new oligosaccharide at the active site demonstrates that SusG can accommodate α1,6 branch points at subsite -3 to -2, and also at subsite+1 adjacent to the site of hydrolysis, explaining how this enzyme may be able to process a wide range of limit dextrins in the intestinal environment. These data suggest that B. thetaiotaomicron and related organisms may have a selective advantage for amylosaccharide scavenging in the gut. PubMed: 29603462DOI: 10.1002/pro.3410 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.17 Å) |
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