5F15

Crystal Structure of ArnT from Cupriavidus metallidurans bound to Undecaprenyl phosphate

5F15 の概要

• エントリーDOI: 10.2210/pdb5f15/pdb
• 関連するPDBエントリー: 5EZM
• 分子名称: 4-amino-4-deoxy-L-arabinose (L-Ara4N) transferase, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (7 entities in total)
• 機能のキーワード: membrane protein, lipid glycosyltransferase, gt-c fold, undecaprenyl phosphate, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, transferase
• 由来する生物種: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 91560.84

構造登録者

Petrou, V.I.,Clarke, O.B.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Mancia, F.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2015-11-30, 公開日: 2016-02-17, 最終更新日: 2024-03-06)

主引用文献

Petrou, V.I.,Herrera, C.M.,Schultz, K.M.,Clarke, O.B.,Vendome, J.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Belcher Dufrisne, M.,Kloss, B.,Kloppmann, E.,Rost, B.,Klug, C.S.,Trent, M.S.,Shapiro, L.,Mancia, F.
Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.
Science, 351:608-612, 2016

PubMed Abstract: Polymyxins are antibiotics used in the last line of defense to combat multidrug-resistant infections by Gram-negative bacteria. Polymyxin resistance arises through charge modification of the bacterial outer membrane with the attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose to lipid A, a reaction catalyzed by the integral membrane lipid-to-lipid glycosyltransferase 4-amino-4-deoxy-L-arabinose transferase (ArnT). Here, we report crystal structures of ArnT from Cupriavidus metallidurans, alone and in complex with the lipid carrier undecaprenyl phosphate, at 2.8 and 3.2 angstrom resolution, respectively. The structures show cavities for both lipidic substrates, which converge at the active site. A structural rearrangement occurs on undecaprenyl phosphate binding, which stabilizes the active site and likely allows lipid A binding. Functional mutagenesis experiments based on these structures suggest a mechanistic model for ArnT family enzymes.

PubMed: 26912703
DOI: 10.1126/science.aad1172

実験手法

X-RAY DIFFRACTION (3.2 Å)