5JW6

Cystal structure of aspartate semialdehyde dehydrogenase from Aspergillus fumigatus

5JW6 の概要

• エントリーDOI: 10.2210/pdb5jw6/pdb
• 分子名称: Aspartate-semialdehyde dehydrogenase, SULFATE ION (3 entities in total)
• 機能のキーワード: rossman fold, oxidoreductase
• 由来する生物種: Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81580.68

構造登録者

Dahal, G.P.,Viola, R.E. (登録日: 2016-05-11, 公開日: 2017-01-11, 最終更新日: 2023-09-27)

主引用文献

Dahal, G.P.,Viola, R.E.
Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus.
Acta Crystallogr F Struct Biol Commun, 73:36-44, 2017

PubMed Abstract: Aspartate-semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate biosynthetic pathway and represents a validated target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of β-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. The absence of this entire pathway in humans and other mammals will allow the selective targeting of pathogenic microorganisms for antimicrobial development. Here, the X-ray structure of a new form of ASADH from the pathogenic fungal species Aspergillus fumigatus has been determined. The overall structure of this enzyme is similar to those of its bacterial orthologs, but there are some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs with selective toxicity against infectious fungal organisms.

PubMed: 28045392
DOI: 10.1107/S2053230X16020070

実験手法

X-RAY DIFFRACTION (2.39 Å)