2NAD

HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE

2NAD の概要

• エントリーDOI: 10.2210/pdb2nad/pdb
• 分子名称: NAD-DEPENDENT FORMATE DEHYDROGENASE, AZIDE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase(aldehyde(d), nad+(a))
• 由来する生物種: Pseudomonas sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88080.74

構造登録者

Lamzin, V.S.,Dauter, Z.,Popov, V.O.,Harutyunyan, E.H.,Wilson, K.S. (登録日: 1994-07-06, 公開日: 1995-01-26, 最終更新日: 2024-02-21)

主引用文献

Lamzin, V.S.,Dauter, Z.,Popov, V.O.,Harutyunyan, E.H.,Wilson, K.S.
High resolution structures of holo and apo formate dehydrogenase.
J.Mol.Biol., 236:759-785, 1994

PubMed Abstract: Three-dimensional crystal structures of holo (ternary complex enzyme-NAD-azide) and apo NAD-dependent dimeric formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 have been refined to R factors of 11.7% and 14.8% at 2.05 and 1.80 A resolution, respectively. The estimated root-mean-square error in atomic co-ordinates is 0.11 A for holo and 0.18 A for apo. X-ray data were collected from single crystals using an imaging plate scanner and synchrotron radiation. In both crystal forms there is a dimer in the asymmetric unit. Both structures show essentially 2-fold molecular symmetry. NAD binding causes movement of the catalytic domain and ordering of the C terminus, where a new helix appears. This completes formation of the enzyme active centre in holo FDH. NAD is bound in the cleft separating the domains and mainly interacts with residues from the co-enzyme binding domain. In apo FDH these residues are held in essentially the same conformation by water molecules occupying the NAD binding region. An azide molecule is located near the point of catalysis, the C4 atom of the nicotinamide moiety of NAD, and overlaps with the proposed formate binding site. There is an extensive channel running from the active site to the protein surface and this is supposed to be used by substrate to reach the active centre after NAD has already bound. The structure of the active site and a hypothetical catalytic mechanism are discussed. Sequence homology of FDH with other NAD-dependent formate dehydrogenases and some D-specific dehydrogenases is discussed on the basis of the FDH three-dimensional structure.

PubMed: 8114093
DOI: 10.1006/jmbi.1994.1188

実験手法

X-RAY DIFFRACTION (2.05 Å)