5U1Z

X-ray structure of the WlarG aminotransferase, apo form, from Campylobacter jejune

5U1Z の概要

• エントリーDOI: 10.2210/pdb5u1z/pdb
• 関連するPDBエントリー: 5U20 5U21 5U23 5U24
• 分子名称: Putative aminotransferase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: aminotransferase, plp, lipooligosaccharide, transferase
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 176330.46

構造登録者

Holden, H.M.,Thoden, J.B.,Dow, G.T.,Gilbert, M. (登録日: 2016-11-29, 公開日: 2017-01-11, 最終更新日: 2023-10-04)

主引用文献

Dow, G.T.,Gilbert, M.,Thoden, J.B.,Holden, H.M.
Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase.
Protein Sci., 26:586-599, 2017

PubMed Abstract: Campylobacter jejuni is a Gram-negative bacterium that represents a leading cause of human gastroenteritis worldwide. Of particular concern is the link between C. jejuni infections and the subsequent development of Guillain-Barré syndrome, an acquired autoimmune disorder leading to paralysis. All Gram-negative bacteria contain complex glycoconjugates anchored to their outer membranes, but in most strains of C. jejuni, this lipoglycan lacks the O-antigen repeating units. Recent mass spectrometry analyses indicate that the C. jejuni 81116 (Penner serotype HS:6) lipoglycan contains two dideoxyhexosamine residues, and enzymological assay data show that this bacterial strain can synthesize both dTDP-3-acetamido-3,6-dideoxy-d-glucose and dTDP-3-acetamido-3,6-dideoxy-d-galactose. The focus of this investigation is on WlaRG from C. jejuni, which plays a key role in the production of these unusual sugars by functioning as a pyridoxal 5'-phosphate dependent aminotransferase. Here, we describe the first three-dimensional structures of the enzyme in various complexes determined to resolutions of 1.7 Å or higher. Of particular significance are the external aldimine structures of WlaRG solved in the presence of either dTDP-3-amino-3,6-dideoxy-d-galactose or dTDP-3-amino-3,6-dideoxy-d-glucose. These models highlight the manner in which WlaRG can accommodate sugars with differing stereochemistries about their C-4' carbon positions. In addition, we present a corrected structure of WbpE, a related sugar aminotransferase from Pseudomonas aeruginosa, solved to 1.3 Å resolution.

PubMed: 28028852
DOI: 10.1002/pro.3109

実験手法

X-RAY DIFFRACTION (1.6 Å)