PDBsum entry 5cef

Oxidoreductase

PDB id: 5cef

Contents

Protein chains

359 a.a.

Ligands

EDO

Waters ×619

PDB id:

5cef

Name:

Oxidoreductase

Title:

Cystal structure of aspartate semialdehyde dehydrogenase from cryptococcus neoformans

Structure:

Aspartate-semialdehyde dehydrogenase. Chain: a, b, c, d. Engineered: yes

Source:

Cryptococcus neoformans var. Neoformans jec21. Organism_taxid: 214684. Gene: cna02450. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.60Å R-factor: 0.183 R-free: 0.220

Authors:

G.P.Dahal,R.E.Viola

Key ref:

G.Dahal and R.E.Viola (2015). Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans. Acta Crystallogr F Struct Biol Commun, 71, 1365-1371. PubMed id: 26527262 DOI: 10.1107/S2053230X15017495

Date:

06-Jul-15 Release date: 18-Nov-15

Protein chains

Q5KPK7  (Q5KPK7_CRYNJ) -  aspartate-semialdehyde dehydrogenase from Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)

Seq: 365 a.a.

Struc: 359 a.a.

Enzyme reactions

• Enzyme class: E.C.1.2.1.11 - aspartate-semialdehyde dehydrogenase.
• Pathway: Lysine biosynthesis (early stages)
• Reaction: L-aspartate 4-semialdehyde + phosphate + NADP⁺ = 4-phospho-L-aspartate + NADPH + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X15017495

Acta Crystallogr F Struct Biol Commun 71:1365-1371 (2015)

PubMed id: 26527262

Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans.

G.Dahal, R.E.Viola.

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.