4ND4

Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor (b-nicotinamide adenine dinucleotide)

「2FM3」から置き換えられました

4ND4 の概要

• エントリーDOI: 10.2210/pdb4nd4/pdb
• 関連するPDBエントリー: 4ND1 4ND2 4ND3 4ND5
• 分子名称: Lactate dehydrogenase, adjacent gene encodes predicted malate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PYRUVIC ACID, ... (5 entities in total)
• 機能のキーワード: rossmann fold, dehydrogenase, nad binding, oxidoreductase
• 由来する生物種: Cryptosporidium parvum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69733.15

構造登録者

Chattopadhyay, D.,Cook, W.J. (登録日: 2013-10-25, 公開日: 2014-12-17, 最終更新日: 2024-11-06)

主引用文献

Cook, W.J.,Senkovich, O.,Hernandez, A.,Speed, H.,Chattopadhyay, D.
Biochemical and structural characterization of Cryptosporidium parvum Lactate dehydrogenase.
Int.J.Biol.Macromol., 74C:608-619, 2014

PubMed Abstract: The protozoan parasite Cryptosporidium parvum causes waterborne diseases worldwide. There is no effective therapy for C. parvum infection. The parasite depends mainly on glycolysis for energy production. Lactate dehydrogenase is a major regulator of glycolysis. This paper describes the biochemical characterization of C. parvum lactate dehydrogenase and high resolution crystal structures of the apo-enzyme and four ternary complexes. The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. The results reveal distinctive features of the parasitic enzyme. For example, C. parvum lactate dehydrogenase prefers the acetylpyridine analog of NADH as a cofactor. Moreover, it is slightly less sensitive to gossypol inhibition compared with mammalian lactate dehydrogenases and not inhibited by excess pyruvate. The active site loop and the antigenic loop in C. parvum lactate dehydrogenase are considerably different from those in the human counterpart. Structural features and enzymatic properties of C. parvum lactate dehydrogenase are similar to enzymes from related parasites. Structural comparison with malate dehydrogenase supports a common ancestry for the two genes.

PubMed: 25542170
DOI: 10.1016/j.ijbiomac.2014.12.019

実験手法

X-RAY DIFFRACTION (2.2 Å)