8DL2

BoGH13ASus from Bacteroides ovatus bound to acarbose

8DL2 の概要

• エントリーDOI: 10.2210/pdb8dl2/pdb
• 関連するPDBエントリー: 8DGE 8DL1
• 関連するBIRD辞書のPRD_ID: PRD_900007
• 分子名称: Alpha amylase, catalytic domain protein, TRIETHYLENE GLYCOL, GLYCEROL, ... (17 entities in total)
• 機能のキーワード: alpha-amylase, starch, gh13, glycoside hydrolase, hydrolase
• 由来する生物種: Bacteroides ovatus ATCC 8483
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 346940.77

構造登録者

Brown, H.A.,DeVeaux, A.L.,Koropatkin, N.M. (登録日: 2022-07-06, 公開日: 2023-05-24, 最終更新日: 2024-04-10)

主引用文献

Brown, H.A.,DeVeaux, A.L.,Juliano, B.R.,Photenhauer, A.L.,Boulinguiez, M.,Bornschein, R.E.,Wawrzak, Z.,Ruotolo, B.T.,Terrapon, N.,Koropatkin, N.M.
BoGH13A Sus from Bacteroides ovatus represents a novel alpha-amylase used for Bacteroides starch breakdown in the human gut.
Cell.Mol.Life Sci., 80:232-232, 2023

PubMed Abstract: Members of the Bacteroidetes phylum in the human colon deploy an extensive number of proteins to capture and degrade polysaccharides. Operons devoted to glycan breakdown and uptake are termed polysaccharide utilization loci or PUL. The starch utilization system (Sus) is one such PUL and was initially described in Bacteroides thetaiotaomicron (Bt). BtSus is highly conserved across many species, except for its extracellular α-amylase, SusG. In this work, we show that the Bacteroides ovatus (Bo) extracellular α-amylase, BoGH13A, is distinguished from SusG in its evolutionary origin and its domain architecture and by being the most prevalent form in Bacteroidetes Sus. BoGH13A is the founding member of both a novel subfamily in the glycoside hydrolase family 13, GH13_47, and a novel carbohydrate-binding module, CBM98. The BoGH13A CBM98-CBM48-GH13_47 architecture differs from the CBM58 embedded within the GH13_36 of SusG. These domains adopt a distinct spatial orientation and invoke a different association with the outer membrane. The BoCBM98 binding site is required for Bo growth on polysaccharides and optimal enzymatic degradation thereof. Finally, the BoGH13A structure features bound Ca and Mn ions, the latter of which is novel for an α-amylase. Little is known about the impact of Mn on gut bacterial function, much less on polysaccharide consumption, but Mn addition to Bt expressing BoGH13A specifically enhances growth on starch. Further understanding of bacterial starch degradation signatures will enable more tailored prebiotic and pharmaceutical approaches that increase starch flux to the gut.

PubMed: 37500984
DOI: 10.1007/s00018-023-04812-w

実験手法

X-RAY DIFFRACTION (1.99 Å)