2IV2

Reinterpretation of reduced form of formate dehydrogenase H from E. coli

2IV2 の概要

• エントリーDOI: 10.2210/pdb2iv2/pdb
• 関連するPDBエントリー: 1AA6 1FDI 1FDO
• 分子名称: Formate dehydrogenase H, IRON/SULFUR CLUSTER, GUANYLATE-O'-PHOSPHORIC ACID MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL) ESTER, ... (7 entities in total)
• 機能のキーワード: oxidoreductase, 4fe-4s, naerobic, dehydrogenase, fe4s4, formate, iron, iron sulfur cluster, iron-sulfur, metal-binding, mgd, molybdenum, molybdopterin, molybdopterin guanine dinucleotide, mpt, nad, secys, selenium, selenocysteine
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81396.41

構造登録者

Raaijmakers, H.C.A.,Romao, M.J. (登録日: 2006-06-08, 公開日: 2006-06-12, 最終更新日: 2023-12-13)

主引用文献

Raaijmakers, H.C.A.,Romao, M.J.
Formate-Reduced E. Coli Formate Dehydrogenase H: The Reinterpretation of the Crystal Structure Suggests a New Reaction Mechanism.
J.Biol.Inorg.Chem., 11:849-, 2006

PubMed Abstract: Re-evaluation of the crystallographic data of the molybdenum-containing E. coli formate dehydrogenase H (Boyington et al. Science 275:1305-1308, 1997), reported in two redox states, reveals important structural differences for the formate-reduced form, with large implications for the reaction mechanism proposed in that work. We have re-refined the reduced structure with revised protocols and found substantial rearrangement in some parts of it. The original model is essentially correct but an important loop close to the molybdenum active site was mistraced, and, therefore, catalytic relevant residues were located in wrong positions. In particular selenocysteine-140, a ligand of molybdenum in the original work, and essential for catalysis, is no longer bound to the metal after reduction of the enzyme with formate. These results are incompatible with the originally proposed reaction mechanism. On the basis of our new interpretation, we have revised and proposed a new reaction mechanism, which reconciles the new X-ray model with previous biochemical and extended X-ray absorption fine structure data.

PubMed: 16830149
DOI: 10.1007/S00775-006-0129-2

実験手法

X-RAY DIFFRACTION (2.27 Å)