5CEF

Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans

Summary for 5CEF

• Entry DOI: 10.2210/pdb5cef/pdb
• Descriptor: Aspartate-semialdehyde dehydrogenase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: rossman fold, oxidoreductase
• Biological source: Cryptococcus neoformans var. neoformans JEC21
• Total number of polymer chains: 4
• Total formula weight: 161326.44

Authors

Dahal, G.P.,Viola, R.E. (deposition date: 2015-07-06, release date: 2015-11-18, Last modification date: 2023-09-27)

Primary citation

Dahal, G.,Viola, R.E.
Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans.
Acta Crystallogr.,Sect.F, 71:1365-1371, 2015

PubMed Abstract: Aspartate semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate-biosynthetic pathway and represents a valid target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of β-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. Production of this intermediate represents the first committed step in the biosynthesis of the essential amino acids methionine, isoleucine and threonine in fungi, and also the amino acid lysine in bacteria. The structure of a new fungal form of ASADH from Cryptococcus neoformans has been determined to 2.6 Å resolution. The overall structure of CnASADH is similar to those of its bacterial orthologs, but with some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs.

PubMed: 26527262
DOI: 10.1107/S2053230X15017495

Experimental method

X-RAY DIFFRACTION (2.6 Å)