1BRM

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI

1BRM の概要

• エントリーDOI: 10.2210/pdb1brm/pdb
• 分子名称: ASPARTATE-SEMIALDEHYDE DEHYDROGENASE (2 entities in total)
• 機能のキーワード: dehydrogenase, escherichia coli, enzyme, nadp, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 120170.21

構造登録者

Hadfield, A.T.,Kryger, G.,Ouyang, J.,Ringe, D.,Petsko, G.A.,Viola, R.E. (登録日: 1998-08-24, 公開日: 1999-06-22, 最終更新日: 2024-02-07)

主引用文献

Hadfield, A.,Kryger, G.,Ouyang, J.,Petsko, G.A.,Ringe, D.,Viola, R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J.Mol.Biol., 289:991-1002, 1999

PubMed Abstract: Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in an essential aspartic biosynthetic pathway found in bacteria, fungi and the higher plants. Mutations in the asd gene encoding for ASADH that produce an inactive enzyme are lethal, which suggests that ASADH may be an effective target for antibacterial, herbicidal and fungicidal agents. We have solved the crystal structure of the Escherichia coli enzyme to 2.5 A resolution using single isomorphous replacement and 3-fold non-crystallographic symmetry. Each monomer has an N-terminal nucleotide-binding domain and a dimerisation domain. The presence of an essential cysteine locates the active site in a cleft between the two domains. The functional dimer has the appearance of a butterfly, with the NADP-binding domains forming the wings and the dimerisation domain forming the body.A histidine residue is identified as a likely acid/base catalyst in the enzymic reaction. Other amino acids implicated in the enzymic activity by mutagenesis are found in the active site region and define the substrate binding pocket.

PubMed: 10369777
DOI: 10.1006/jmbi.1999.2828

実験手法

X-RAY DIFFRACTION (2.5 Å)