6ABJ

The apo-structure of D-lactate dehydrogenase from Pseudomonas aeruginosa

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6ABJ の概要

• エントリーDOI: 10.2210/pdb6abj/pdb
• 分子名称: D-lactate dehydrogenase (Fermentative), ACETATE ION (3 entities in total)
• 機能のキーワード: rossmann fold, dehydrogenase, nadh binding, oxidoreductase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75783.60

構造登録者

Furukawa, N.,Miyanaga, A.,Nakajima, M.,Taguchi, H. (登録日: 2018-07-21, 公開日: 2018-09-19, 最終更新日: 2025-03-12)

主引用文献

Furukawa, N.,Miyanaga, A.,Nakajima, M.,Taguchi, H.
Structural Basis of Sequential Allosteric Transitions in Tetrameric d-Lactate Dehydrogenases from Three Gram-Negative Bacteria
Biochemistry, 57:5388-5406, 2018

PubMed Abstract: d-Lactate dehydrogenases (d-LDHs) from Fusobacterium nucleatum (FnLDH) and Escherichia coli (EcLDH) exhibit positive cooperativity in substrate binding, and the Pseudomonas aeruginosa enzyme (PaLDH) shows negatively cooperative substrate binding. The apo and ternary complex structures of FnLDH and PaLDH have been determined together with the apo-EcLDH structure. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, unlike Lactobacillus d-LDHs, P-axis-related dimeric enzymes, although apo-FnLDH and EcLDH form asymmetric and distorted quaternary structures. The tetrameric structure allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. These contact surfaces comprise intersubunit hydrogen bonds and hydrophobic interactions and likely prevent the domain closure motion during initial substrate binding. In contrast, apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains, which present their negatively charged surfaces to each other at the subunit interface. Complex FnLDH and PaLDH possess highly symmetrical quaternary structures with closed forms of the catalytic domains, which are separate from each other at the subunit interface. Structure-based mutations successfully converted the three enzymes to their dimeric forms, which exhibited no significant cooperativity in substrate binding. These observations indicate that the three enzymes undergo typical sequential allosteric transitions to exhibit their distinctive allosteric functions through the tetrameric structures.

PubMed: 30149697
DOI: 10.1021/acs.biochem.8b00557

実験手法

X-RAY DIFFRACTION (1.86 Å)