1DIH

THREE-DIMENSIONAL STRUCTURE OF E. COLI DIHYDRODIPICOLINATE REDUCTASE

1DIH の概要

• エントリーDOI: 10.2210/pdb1dih/pdb
• 分子名称: DIHYDRODIPICOLINATE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29539.05

構造登録者

Scapin, G.,Blanchard, J.S.,Sacchettini, J.C. (登録日: 1994-09-14, 公開日: 1995-09-15, 最終更新日: 2024-02-07)

主引用文献

Scapin, G.,Blanchard, J.S.,Sacchettini, J.C.
Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase.
Biochemistry, 34:3502-3512, 1995

PubMed Abstract: Dihydrodipicolinate reductase is an enzyme found in bacteria and higher plants involved in the biosynthesis of diaminopimelic acid and lysine. Because these pathways are unique to bacteria and plants, they may represent attractive targets for new antimicrobial or herbicidal compounds. The three-dimensional structure of Escherichia coli dihydrodipicolinate reductase, complexed with NADPH, has been determined and refined to a crystallographic R-factor of 18.6% with diffraction data to 2.2 A resolution. The refined model contains the complete protein chain, the cofactor NADPH, and 55 water molecules. The enzyme is composed of two domains. The dinucleotide binding domain has a central seven-stranded parallel beta-sheet surrounded by four alpha-helices, with the cofactor binding site located at the carboxy-terminal edge of the sheet. The second domain contains four beta-strands and two alpha-helices that form an open mixed beta-sandwich. A possible binding site for dihydrodipicolinate has been identified in this second domain, about 12 A away from the dinucleotide binding site. This would imply that the protein must undergo some conformational change in order to perform catalysis. In the crystal, the native enzyme is a homotetramer generated by a 222 crystallographic axis. Implications of the tetrameric structure for the enzyme function are presented. Dihydrodipicolinate reductase uses both NADH and NADPH as cofactors, and analysis of its cofactor binding site allows for a molecular understanding of the enzyme's dual specificity.

PubMed: 7893645
DOI: 10.1021/bi00011a003

実験手法

X-RAY DIFFRACTION (2.2 Å)