5DCE

Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase regulated (Tryptophan)

5DCE の概要

• エントリーDOI: 10.2210/pdb5dce/pdb
• 関連するPDBエントリー: 5DCC 5DCD
• 分子名称: Phospho-2-dehydro-3-deoxyheptonate aldolase, MANGANESE (II) ION, TRYPTOPHAN, ... (4 entities in total)
• 機能のキーワード: allostery, aromatic amino acids, dah7ps, transferase
• 由来する生物種: Neisseria meningitidis serogroup B (strain MC58)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155885.18

構造登録者

Heyes, L.C.,Parker, E.J. (登録日: 2015-08-24, 公開日: 2016-08-24, 最終更新日: 2024-03-06)

主引用文献

Cross, P.J.,Heyes, L.C.,Zhang, S.,Nazmi, A.R.,Parker, E.J.
The Functional Unit of Neisseria meningitidis 3-Deoxy--Arabino-Heptulosonate 7-Phosphate Synthase Is Dimeric.
Plos One, 11:e0145187-e0145187, 2016

PubMed Abstract: Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (NmeDAH7PS) adopts a homotetrameric structure consisting of an extensive and a less extensive interface. Perturbation of the less extensive interface through a single mutation of a salt bridge (Arg126-Glu27) formed at the tetramer interface of all chains resulted in a dimeric DAH7PS in solution, as determined by small angle X-ray scattering, analytical ultracentrifugation and analytical size-exclusion chromatography. The dimeric NmeDAH7PSR126S variant was shown to be catalytically active in the aldol-like condensation reaction between D-erythrose 4-phosphate and phosphoenolpyruvate, and allosterically inhibited by L-phenylalanine to the same extent as the wild-type enzyme. The dimeric NmeDAH7PSR126S variant exhibited a slight reduction in thermal stability by differential scanning calorimetry experiments and a slow loss of activity over time compared to the wild-type enzyme. Although NmeDAH7PSR126S crystallised as a tetramer, like the wild-type enzyme, structural asymmetry at the less extensive interface was observed consistent with its destabilisation. The tetrameric association enabled by this Arg126-Glu27 salt-bridge appears to contribute solely to the stability of the protein, ultimately revealing that the functional unit of NmeDAH7PS is dimeric.

PubMed: 26828675
DOI: 10.1371/journal.pone.0145187

実験手法

X-RAY DIFFRACTION (2.23 Å)