1YS4

Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii

1YS4 の概要

• エントリーDOI: 10.2210/pdb1ys4/pdb
• 関連するPDBエントリー: 1BRM 1NWC
• 分子名称: Aspartate-semialdehyde dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, MALONIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, asadh
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81821.76

構造登録者

Faehnle, C.R.,Ohren, J.F.,Viola, R.E. (登録日: 2005-02-07, 公開日: 2005-11-01, 最終更新日: 2024-10-30)

主引用文献

Faehnle, C.R.,Ohren, J.F.,Viola, R.E.
A New Branch in the Family: Structure of Aspartate-beta-semialdehyde Dehydrogenase from Methanococcus jannaschii
J.Mol.Biol., 353:1055-1068, 2005

PubMed Abstract: The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Methanococcus jannaschii has been determined to 2.3 angstroms resolution using multiwavelength anomalous diffraction (MAD) phasing of a selenomethionine-substituted derivative to define a new branch in the family of ASADHs. This new structure has a similar overall fold and domain organization despite less than 10% conserved sequence identity with the bacterial enzymes. However, the entire repertoire of functionally important active site amino acid residues is conserved, suggesting an identical catalytic mechanism but with lower catalytic efficiency. A new coenzyme-binding conformation and dual NAD/NADP coenzyme specificity further distinguish this archaeal branch from the bacterial ASADHs. Several structural differences are proposed to account for the dramatically enhanced thermostability of this archaeal enzyme. Finally, the intersubunit communication channel connecting the active sites in the bacterial enzyme dimer has been disrupted in the archaeal ASADHs by amino acid changes that likely prevent the alternating sites reactivity previously proposed for the bacterial ASADHs.

PubMed: 16225889
DOI: 10.1016/j.jmb.2005.09.027

実験手法

X-RAY DIFFRACTION (2.29 Å)