4R36

Crystal structure analysis of LpxA, a UDP-N-acetylglucosamine acyltransferase from Bacteroides fragilis 9343

4R36 の概要

• エントリーDOI: 10.2210/pdb4r36/pdb
• 関連するPDBエントリー: 4R37
• 分子名称: Putative acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, 2-(2-METHOXYETHOXY)ETHANOL, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: left-handed beta helix, udp-n-acetylglucosamine acyltransferase, transferase
• 由来する生物種: Bacteroides fragilis
• 細胞内の位置: Cytoplasm : Q5LH16
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60689.15

構造登録者

Ngo, A.,Fong, K.,Cox, D.,Fisher, A.,Chen, X. (登録日: 2014-08-14, 公開日: 2015-05-06, 最終更新日: 2023-09-20)

主引用文献

Ngo, A.,Fong, K.T.,Cox, D.L.,Chen, X.,Fisher, A.J.
Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA).
Acta Crystallogr.,Sect.D, 71:1068-1076, 2015

PubMed Abstract: Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. Lipid A constitutes a major component of lipopolysaccharides, also referred to as endotoxins, which form the outer monolayer of the outer membrane of Gram-negative bacteria. Ligand-free and UDP-GlcNAc-bound crystal structures of LpxA from Bacteroides fragilis NCTC 9343, the most common pathogenic bacteria found in abdominal abscesses, have been determined and are presented here. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-rung left-handed β-helical (LβH) fold in the N-terminus followed by an α-helical motif in the C-terminus. The structure is highly similar to LpxA from other organisms. Yet, despite sharing a similar LβH structure with LpxAs from Escherichia coli and others, previously unseen calcium ions are observed on the threefold axis in B. fragilis LpxA to help stabilize the trimeric assembly.

PubMed: 25945572
DOI: 10.1107/S1399004715003326

実験手法

X-RAY DIFFRACTION (1.9 Å)