5EKE

Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant)

5EKE の概要

• エントリーDOI: 10.2210/pdb5eke/pdb
• 関連するPDBエントリー: 5EKP
• 分子名称: Uncharacterized glycosyltransferase sll0501, URIDINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: glycosyltransferase, membrane protein, enzyme, bactoprenol, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, transferase
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158687.21

構造登録者

Ardiccioni, C.,Clarke, O.B.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Liu, Q.,Shapiro, L.,Mancia, F.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2015-11-03, 公開日: 2016-01-06, 最終更新日: 2024-03-06)

主引用文献

Ardiccioni, C.,Clarke, O.B.,Tomasek, D.,Issa, H.A.,von Alpen, D.C.,Pond, H.L.,Banerjee, S.,Rajashankar, K.R.,Liu, Q.,Guan, Z.,Li, C.,Kloss, B.,Bruni, R.,Kloppmann, E.,Rost, B.,Manzini, M.C.,Shapiro, L.,Mancia, F.
Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis.
Nat Commun, 7:10175-10175, 2016

PubMed Abstract: The attachment of a sugar to a hydrophobic polyisoprenyl carrier is the first step for all extracellular glycosylation processes. The enzymes that perform these reactions, polyisoprenyl-glycosyltransferases (PI-GTs) include dolichol phosphate mannose synthase (DPMS), which generates the mannose donor for glycosylation in the endoplasmic reticulum. Here we report the 3.0 Å resolution crystal structure of GtrB, a glucose-specific PI-GT from Synechocystis, showing a tetramer in which each protomer contributes two helices to a membrane-spanning bundle. The active site is 15 Å from the membrane, raising the question of how water-soluble and membrane-embedded substrates are brought into apposition for catalysis. A conserved juxtamembrane domain harbours disease mutations, which compromised activity in GtrB in vitro and in human DPM1 tested in zebrafish. We hypothesize a role of this domain in shielding the polyisoprenyl-phosphate for transport to the active site. Our results reveal the basis of PI-GT function, and provide a potential molecular explanation for DPM1-related disease.

PubMed: 26729507
DOI: 10.1038/ncomms10175

実験手法

X-RAY DIFFRACTION (3.001 Å)