1YL7

the crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) in complex with NADH (crystal form C)

1YL7 の概要

• エントリーDOI: 10.2210/pdb1yl7/pdb
• 関連するPDBエントリー: 1YL5 1YL6
• 分子名称: Dihydrodipicolinate reductase, MAGNESIUM ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: lysine biosynthesis, dihydrodipicolinate, reductase, nadh, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, oxidoreductase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 211095.28

構造登録者

Janowski, R.,Kefala, G.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (登録日: 2005-01-19, 公開日: 2006-01-17, 最終更新日: 2023-08-23)

主引用文献

Janowski, R.,Kefala, G.,Weiss, M.S.
The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms.
Acta Crystallogr.,Sect.D, 66:61-72, 2010

PubMed Abstract: Dihydrodipicolinate reductase (DHDPR, DapB) is an enzyme that belongs to the L-lysine biosynthetic pathway. DHDPR reduces the alpha,beta-unsaturated cyclic imine 2,3-dihydrodipicolinic acid to yield the compound 2,3,4,5-tetrahydrodipicolinic acid in a pyridine nucleotide-dependent reaction. The substrate of this reaction is the unstable product of the preceding enzyme dihydrodipicolinate synthase (DHDPS, DapA). Here, the structure of apo-DHDPR from Mycobacterium tuberculosis is reported in two orthorhombic crystal forms, as well as the structure of DHDPR from M. tuberculosis in complex with NADH in a monoclinic crystal form. A comparison of the results with previously solved structures of this enzyme shows that DHDPR undergoes a major conformational change upon binding of its cofactor. This conformational change can be interpreted as one of the low-frequency normal modes of the structure.

PubMed: 20057050
DOI: 10.1107/S0907444909043960

実験手法

X-RAY DIFFRACTION (2.34 Å)