6BDX

4-hydroxy tetrahydrodipicolinate reductase from Neisseria gonorrhoeae

6BDX の概要

• エントリーDOI: 10.2210/pdb6bdx/pdb
• 分子名称: 4-hydroxy-tetrahydrodipicolinate reductase, SULFATE ION (3 entities in total)
• 機能のキーワード: lysine biosynthesis, 4-hydroxy tetrahydrodipicolinate reductase, neisseria gonorrhoeae, oxidoreductase
• 由来する生物種: Neisseria gonorrhoeae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29130.67

構造登録者

Pote, S.S.,Pye, S.E.,Sheahan, T.E.,Chruszcz, M. (登録日: 2017-10-24, 公開日: 2018-08-29, 最終更新日: 2023-10-04)

主引用文献

Pote, S.,Pye, S.E.,Sheahan, T.E.,Gawlicka-Chruszcz, A.,Majorek, K.A.,Chruszcz, M.
4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog.
Biochem. Biophys. Res. Commun., 503:1993-1999, 2018

PubMed Abstract: Neisseria gonorrhoeae, an obligate human pathogen, is a leading cause of communicable diseases globally. Due to rapid development of drug resistance, the rate of successfully curing gonococcal infections is rapidly decreasing. Hence, research is being directed toward finding alternative drugs or drug targets to help eradicate these infections. 4-Hydroxy-tetrahydrodipicolinate reductase (DapB), an important enzyme in the meso-diaminopimelate pathway, is a promising target for the development of new antibiotics. This manuscript describes the first structure of DapB from N. gonorrhoeae determined at 1.85 Å. This enzyme uses NAD(P)H as cofactor. Details of the interactions of the enzyme with its cofactors and a substrate analog/inhibitor are discussed. A large scale bioinformatics analysis of DapBs' sequences is also described.

PubMed: 30093108
DOI: 10.1016/j.bbrc.2018.07.147

実験手法

X-RAY DIFFRACTION (1.85 Å)