EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Mechanistic snapshots of lipid-linked sugar transfer.
ジャーナル・号・ページ	Nat Commun, Vol. 16, Issue 1, Page 11044, Year 2025
掲載日	2025年12月6日
著者	Ryan T Morgan / Stefano Motta / Eva Gil-Iturbe / Biddut Bhattacharjee / Mohammad T Anwar / Giovanni Di Muccio / Alice Romagnoli / Bedangshu Mishra / Khuram U Ashraf / Injin Bang / Daniele Di Marino / Todd L Lowary / Matthias Quick / Vasileios I Petrou / Michael H B Stowell / Rie Nygaard / Filippo Mancia /
PubMed 要旨	Enzymes undergo dynamic conformational changes during catalysis, yet conventional high-resolution structural methods typically capture only the most stable states. Here, we address this gap using ...Enzymes undergo dynamic conformational changes during catalysis, yet conventional high-resolution structural methods typically capture only the most stable states. Here, we address this gap using rapid UV photolysis of a chemically caged substrate with cryogenic time-resolved electron microscopy (cryo-TREM). We elucidate the catalytic mechanism of GtrB, a membrane-bound glycosyltransferase that transfers glucose from UDP-glucose to the lipid carrier undecaprenyl phosphate. We visualized how GtrB, which has an active site ~15 Å from the membrane, transitions during the catalytic cycle to move each substrate in proximity for catalysis. From a single dataset, we resolved distinct conformational states: the initial substrate-bound state, a catalytically poised intermediate, and the product-bound state. Through molecular dynamics simulations and biochemical analyses, we identify coordinated movements within the active site that drive catalysis. These findings provide a molecular framework for understanding how glycosyltransferases function and highlight a broadly applicable strategy for capturing dynamic enzymatic states in native-like environments.
リンク	Nat Commun / PubMed:41353435 / PubMed Central
手法	EM (単粒子)
解像度	2.54 - 3.19 Å
構造データ	49930 9nyc EMDB-49930, PDB-9nyc: Cryo-EM structure of the glycosyltransferase GtrB in the substrate-bound state 手法: EM (単粒子) / 解像度: 2.54 Å 49931 9nyd EMDB-49931, PDB-9nyd: Cryo-EM structure of the glycosyltransferase GtrB in the pre-catalysis and product-bound state 手法: EM (単粒子) / 解像度: 2.85 Å 49932 9nye EMDB-49932, PDB-9nye: Cryo-EM structure of the glycosyltransferase GtrB in the apo state (octamer volume) 手法: EM (単粒子) / 解像度: 2.79 Å 49933 9nyf EMDB-49933, PDB-9nyf: Cryo-EM structure of the glycosyltransferase GtrB (tetramer volume) 手法: EM (単粒子) / 解像度: 3.19 Å 49935 9nyk EMDB-49935, PDB-9nyk: Cryo-EM structure of the glycosyltransferase GtrB in the pre-intermediate state 手法: EM (単粒子) / 解像度: 2.98 Å
化合物	ChemComp-UPG: URIDINE-5'-DIPHOSPHATE-GLUCOSE / UDP-グルコ-ス ChemComp-5TR: [(2~{E},6~{E},10~{E},14~{E},18~{Z},22~{E},26~{Z},30~{E},34~{E},38~{E})-3,7,11,15,19,23,27,31,35,39,43-undecamethyltetratetraconta-2,6,10,14,18,22,26,30,34,38,42-undecaenyl] dihydrogen phosphate ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-UDP: URIDINE-5'-DIPHOSPHATE / UDP / UDPYM PDB-1b94*: RESTRICTION ENDONUCLEASE ECORV WITH CALCIUM
由来	synechocystis sp. pcc 6803 substr. kazusa (バクテリア)
キーワード	MEMBRANE PROTEIN / glycosyltransferase / polyisoprenyl