2IYO

Structural characterization of a bacterial 6PDH reveals aspects of specificity, mechanism and mode of inhibition

2IYO の概要

• エントリーDOI: 10.2210/pdb2iyo/pdb
• 関連するPDBエントリー: 2IYP 2IZ0 2IZ1
• 分子名称: 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING, 6-PHOSPHOGLUCONIC ACID, CACODYLATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, 6-phosphogluconate dehydrogenase, nadp, pentose shunt, gluconate utilization
• 由来する生物種: LACTOCOCCUS LACTIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52914.34

構造登録者

Sundaramoorthy, R.,Iulek, J.,Hunter, W.N. (登録日: 2006-07-21, 公開日: 2007-01-23, 最終更新日: 2023-12-13)

主引用文献

Sundaramoorthy, R.,Iulek, J.,Barrett, M.P.,Bidet, O.,Ruda, G.F.,Gilbert, I.H.,Hunter, W.N.
Crystal Structures of a Bacterial 6-Phosphogluconate Dehydrogenase Reveal Aspects of Specificity, Mechanism and Mode of Inhibition by Analogues of High-Energy Reaction Intermediates.
FEBS J., 274:275-, 2007

PubMed Abstract: Crystal structures of recombinant Lactococcus lactis 6-phosphogluconate dehydrogenase (LlPDH) in complex with substrate, cofactor, product and inhibitors have been determined. LlPDH shares significant sequence identity with the enzymes from sheep liver and the protozoan parasite Trypanosoma brucei for which structures have been reported. Comparisons indicate that the key residues in the active site are highly conserved, as are the interactions with the cofactor and the product ribulose 5-phosphate. However, there are differences in the conformation of the substrate 6-phosphogluconate which may reflect distinct states relevant to catalysis. Analysis of the complex formed with the potent inhibitor 4-phospho-d-erythronohydroxamic acid, suggests that this molecule does indeed mimic the high-energy intermediate state that it was designed to. The analysis also identified, as a contaminant by-product of the inhibitor synthesis, 4-phospho-d-erythronamide, which binds in similar fashion. LlPDH can now serve as a model system for structure-based inhibitor design targeting the enzyme from Trypanosoma species.

PubMed: 17222187
DOI: 10.1111/J.1742-4658.2006.05585.X

実験手法

X-RAY DIFFRACTION (2.4 Å)