6GNF

Granule Bound Starch Synthase from Cyanobacterium sp. CLg1 bound to acarbose and ADP

6GNF の概要

• エントリーDOI: 10.2210/pdb6gnf/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900022
• 分子名称: Glycogen synthase, 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: glycosyl transferase, starch synthase, acarbose, adp, transferase
• 由来する生物種: Cyanobacterium sp. CLg1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 184269.25

構造登録者

Cuesta-Seijo, J.A.,Nielsen, M.M.,Palcic, M.M. (登録日: 2018-05-30, 公開日: 2018-07-25, 最終更新日: 2024-01-17)

主引用文献

Nielsen, M.M.,Ruzanski, C.,Krucewicz, K.,Striebeck, A.,Cenci, U.,Ball, S.G.,Palcic, M.M.,Cuesta-Seijo, J.A.
Crystal Structures of theCatalyticDomain ofArabidopsis thalianaStarch Synthase IV, of Granule Bound Starch Synthase From CLg1 and of Granule Bound Starch Synthase I ofCyanophora paradoxaIllustrate Substrate Recognition in Starch Synthases.
Front Plant Sci, 9:1138-1138, 2018

PubMed Abstract: Starch synthases (SSs) are responsible for depositing the majority of glucoses in starch. Structural knowledge on these enzymes that is available from the crystal structures of rice granule bound starch synthase (GBSS) and barley SSI provides incomplete information on substrate binding and active site architecture. Here we report the crystal structures of the catalytic domains of SSIV from , of GBSS from the cyanobacterium CLg1 and GBSSI from the glaucophyte , with all three bound to ADP and the inhibitor acarbose. The SSIV structure illustrates in detail the modes of binding for both donor and acceptor in a plant SS. CLg1GBSS contains, in the same crystal structure, examples of molecules with and without bound acceptor, which illustrates the conformational changes induced upon acceptor binding that presumably precede catalytic activity. With structures available from several isoforms of plant and non-plant SSs, as well as the closely related bacterial glycogen synthases, we analyze, at the structural level, the common elements that define a SS, the elements that are necessary for substrate binding and singularities of the GBSS family that could underlie its processivity. While the phylogeny of the SSIII/IV/V has been recently discussed, we now further report the detailed evolutionary history of the GBSS/SSI/SSII type of SSs enlightening the origin of the GBSS enzymes used in our structural analysis.

PubMed: 30123236
DOI: 10.3389/fpls.2018.01138

実験手法

X-RAY DIFFRACTION (2.2 Å)