5JW6

Cystal structure of aspartate semialdehyde dehydrogenase from Aspergillus fumigatus

Summary for 5JW6

• Entry DOI: 10.2210/pdb5jw6/pdb
• Descriptor: Aspartate-semialdehyde dehydrogenase, SULFATE ION (3 entities in total)
• Functional Keywords: rossman fold, oxidoreductase
• Biological source: Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
• Total number of polymer chains: 2
• Total formula weight: 81580.68

Authors

Dahal, G.P.,Viola, R.E. (deposition date: 2016-05-11, release date: 2017-01-11, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.39 Å)