› 4ply

X-ray diffraction
1.9Å resolution

Crystal structure of ancestral apicomplexan malate dehydrogenase with malate.

Released:
DOI: 10.2210/pdb4ply/pdb
PDB entry 4ply coloured by chain, front view.
PDB entry 4ply coloured by chain, side view.
PDB entry 4ply coloured by chain, top view.
Source organism: Apicomplexa
Primary publication:
An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
Boucher JI, Jacobowitz JR, Beckett BC, Classen S, Theobald DL
Elife 3 (2014)
PMID: 24966208

Function and Biology Details

Reaction catalysed: 
(S)-lactate + NAD(+) = pyruvate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100444 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 331 amino acids
Theoretical weight: 36.46 KDa
Source organism: Apicomplexa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A075B5H0 (Residues: 1-331; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 8 x NAI
1 bound ligand:
Ligand PYR 6 x PYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P1
Unit cell:
a: 59.311Å b: 90.688Å c: 136.304Å
α: 90.01° β: 90.01° γ: 71.44°
R-values:
R R work R free
0.19 0.189 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

A mechanistic view of enzyme evolution.
Yang et al. (2020)
2 more

1 mention without citation

An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
Boucher et al. (2014)