1B8P

MALATE DEHYDROGENASE FROM AQUASPIRILLUM ARCTICUM

1B8P の概要

• エントリーDOI: 10.2210/pdb1b8p/pdb
• 分子名称: PROTEIN (MALATE DEHYDROGENASE) (2 entities in total)
• 機能のキーワード: dehydrogenase, oxidoreductase
• 由来する生物種: Aquaspirillum arcticum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35287.33

構造登録者

Kim, S.Y.,Hwang, K.Y.,Kim, S.-H.,Han, Y.S.,Cho, Y. (登録日: 1999-02-02, 公開日: 1999-07-09, 最終更新日: 2023-12-27)

主引用文献

Kim, S.Y.,Hwang, K.Y.,Kim, S.H.,Sung, H.C.,Han, Y.S.,Cho, Y.
Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.
J.Biol.Chem., 274:11761-11767, 1999

PubMed Abstract: Aquaspillium arcticum is a psychrophilic bacterium that was isolated from arctic sediment and grows optimally at 4 degrees C. We have cloned, purified, and characterized malate dehydrogenase from A. arcticum (Aa MDH). We also have determined the crystal structures of apo-Aa MDH, Aa MDH.NADH binary complex, and Aa MDH.NAD.oxaloacetate ternary complex at 1.9-, 2.1-, and 2.5-A resolutions, respectively. The Aa MDH sequence is most closely related to the sequence of a thermophilic MDH from Thermus flavus (Tf MDH), showing 61% sequence identity and over 90% sequence similarity. Stability studies show that Aa MDH has a half-life of 10 min at 55 degrees C, whereas Tf MDH is fully active at 90 degrees C for 1 h. Aa MDH shows 2-3-fold higher catalytic efficiency compared with a mesophilic or a thermophilic MDH at the temperature range 4-10 degrees C. Structural comparison of Aa MDH and Tf MDH suggests that the increased relative flexibility of active site residues, favorable surface charge distribution for substrate and cofactor, and the reduced intersubunit ion pair interactions may be the major factors for the efficient catalytic activity of Aa MDH at low temperatures.

PubMed: 10206992
DOI: 10.1074/jbc.274.17.11761

実験手法

X-RAY DIFFRACTION (1.9 Å)