› 3kh5

X-ray diffraction
2.1Å resolution

Crystal Structure of Protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homolog of g-AMPK.

Released:
DOI: 10.2210/pdb3kh5/pdb
PDB entry 3kh5 coloured by chain, front view.
PDB entry 3kh5 coloured by chain, side view.
PDB entry 3kh5 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPK.
Gómez-García I, Oyenarte I, Martínez-Cruz LA
J Mol Biol 399 53-70 (2010)
PMID: 20382158

Function and Biology Details

Reaction catalysed: 
(R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein MJ1225 Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.76 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58622 (Residues: 1-280; Coverage: 100%)
Gene name: MJ1225
Sequence domains: CBS domain
Structure domains: CBS-domain

Ligands and Environments

3 bound ligands:
Ligand ADP 3 x ADP
Ligand AMP 2 x AMP
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: R32
Unit cell:
a: 108.548Å b: 108.548Å c: 143.627Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.228 0.294
Expression system: Escherichia coli

Quick links

Citations

2 review citations

CBS domains: Ligand binding sites and conformational variability.
Ereño-Orbea et al. (2013)
1 more

3 mentions without citation

Chromophorylation of cyanobacteriochrome Slr1393 from Synechocystis sp. PCC 6803 is regulated by protein Slr2111 through allosteric interaction.
He et al. (2018)
2 more