› 1hlp

X-ray diffraction
3.2Å resolution

STRUCTURAL FEATURES STABILIZING HALOPHILIC MALATE DEHYDROGENASE FROM AN ARCHAEBACTERIUM

Released:
DOI: 10.2210/pdb1hlp/pdb
PDB entry 1hlp coloured by chain, front view.
PDB entry 1hlp coloured by chain, side view.
PDB entry 1hlp coloured by chain, top view.
Source organism: Haloarcula marismortui
Primary publication:
Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium.
Dym O, Mevarech M, Sussman JL
Science 267 1344-6 (1995)
PMID: 17812611

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170549 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 32.71 KDa
Source organism: Haloarcula marismortui
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07841 (Residues: 2-304; Coverage: 100%)
Gene names: mdh, rrnAC2706
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 114.6Å b: 130.6Å c: 123.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.28
Expression system: Escherichia coli

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Citations

14 review citations

Na+ tolerance and Na+ transport in higher plants.
Tester et al. (2003)
13 more