3FLU

Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis

3FLU の概要

• エントリーDOI: 10.2210/pdb3flu/pdb
• 関連するPDBエントリー: 1YXC 1YXD
• 分子名称: Dihydrodipicolinate synthase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: tim barrel, beta-alpha-barrel, amino-acid biosynthesis, diaminopimelate biosynthesis, lyase, lysine biosynthesis, schiff base
• 由来する生物種: Neisseria meningitidis serogroup B
• 細胞内の位置: Cytoplasm : Q9JZR4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130559.97

構造登録者

Devenish, S.R.A.,Hadfield, A.T. (登録日: 2008-12-19, 公開日: 2009-06-23, 最終更新日: 2023-11-01)

主引用文献

Devenish, S.R.A.,Huisman, F.H.A.,Parker, E.J.,Hadfield, A.T.,Gerrard, J.A.
Cloning and characterisation of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis.
Biochim.Biophys.Acta, 2009

PubMed Abstract: Neisseria meningitidis is an obligate commensal bacterium of humans, and also an important human pathogen. To facilitate future drug studies, we report here the biochemical and structural characterisation of a key enzyme in (S)-lysine biosynthesis, dihydrodipicolinate synthase (DHDPS), from N. meningitidis (NmeDHDPS). X-ray crystallography revealed only minor structural differences between NmeDHDPS and the enzyme from E. coli at the active and allosteric effector sites. The catalytic capabilities of NmeDHDPS are similar to those of the enzyme from E. coli, but intriguingly NmeDHDPS is subject to substrate inhibition by high concentrations of the second substrate, (S)-aspartate semialdehyde, and is also significantly more sensitive to feedback inhibition by (S)-lysine. This heightened sensitivity to inhibition at both active and allosteric sites suggests that it may be possible to target DHDPS from N. meningitidis for antibiotic development.

PubMed: 19236959
DOI: 10.1016/j.bbapap.2009.02.003

実験手法

X-RAY DIFFRACTION (2 Å)