1LUA

Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 complexed with NADP

1LUA の概要

• エントリーDOI: 10.2210/pdb1lua/pdb
• 関連するPDBエントリー: 1LU9
• 分子名称: Methylene Tetrahydromethanopterin Dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha/beta twisted open sheet structure, oxidoreductase
• 由来する生物種: Methylobacterium extorquens
• 細胞内の位置: Cytoplasm: P55818
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91152.04

構造登録者

Ermler, U.,Hagemeier, C.H.,Roth, A.,Demmer, U.,Grabarse, W.,Warkentin, E.,Vorholt, J.A. (登録日: 2002-05-22, 公開日: 2002-09-11, 最終更新日: 2024-04-03)

主引用文献

Ermler, U.,Hagemeier, C.H.,Roth, A.,Demmer, U.,Grabarse, W.,Warkentin, E.,Vorholt, J.A.
Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1.
Structure, 10:1127-1137, 2002

PubMed Abstract: NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 A resolution. The enzyme is present as a homotrimer. The alpha,beta fold of the monomer is related to that of methylene-H(4)F dehydrogenases, suggesting a common evolutionary origin. The position of the active site is located within a large crevice built up by the two domains of one subunit and one domain of a second subunit. Methylene-H(4)MPT could be modeled into the cleft, and crucial active site residues such as Phe18, Lys256, His260, and Thr102 were identified. The molecular basis of the different substrate specificities and different catalytic demands of MtdA compared to methylene-H(4)F dehydrogenases are discussed.

PubMed: 12176390
DOI: 10.1016/S0969-2126(02)00802-X

実験手法

X-RAY DIFFRACTION (1.9 Å)