6U01

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site

6U01 の概要

• エントリーDOI: 10.2210/pdb6u01/pdb
• 分子名称: 4-hydroxy-tetrahydrodipicolinate synthase, 1,2-ETHANEDIOL, TETRAETHYLENE GLYCOL, ... (9 entities in total)
• 機能のキーワード: dihydrodipicolinate synthase, tim barrel, tetrameric protein, lyase
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 207293.45

構造登録者

Saran, S.,Majdi Yazdi, M.,Lehnert, L.,Palmer, D.R.J.,Sanders, D.A.R. (登録日: 2019-08-13, 公開日: 2019-12-04, 最終更新日: 2023-11-29)

主引用文献

Majdi Yazdi, M.,Saran, S.,Mrozowich, T.,Lehnert, C.,Patel, T.R.,Sanders, D.A.R.,Palmer, D.R.J.
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase.
J.Struct.Biol., 209:107409-107409, 2020

PubMed Abstract: Dihydrodipicolinate synthase (DHDPS) from Campylobacter jejuni is a natively homotetrameric enzyme that catalyzes the first unique reaction of (S)-lysine biosynthesis and is feedback-regulated by lysine through binding to an allosteric site. High-resolution structures of the DHDPS-lysine complex have revealed significant insights into the binding events. One key asparagine residue, N84, makes hydrogen bonds with both the carboxyl and the α-amino group of the bound lysine. We generated two mutants, N84A and N84D, to study the effects of these changes on the allosteric site properties. However, under normal assay conditions, N84A displayed notably lower catalytic activity, and N84D showed no activity. Here we show that these mutations disrupt the quaternary structure of DHDPS in a concentration-dependent fashion, as demonstrated by size-exclusion chromatography, multi-angle light scattering, dynamic light scattering, small-angle X-ray scattering (SAXS) and high-resolution protein crystallography.

PubMed: 31678256
DOI: 10.1016/j.jsb.2019.107409

実験手法

X-RAY DIFFRACTION (1.87 Å)