› 2mv3

Solution NMR

The N-domain of the AAA metalloproteinase Yme1 from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb2mv3/pdb
PDB entry 2mv3 coloured by chain, ensemble of 23 models, front view.
PDB entry 2mv3 coloured by chain, ensemble of 23 models, side view.
PDB entry 2mv3 coloured by chain, ensemble of 23 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure and evolution of N-domains in AAA metalloproteases.
Scharfenberg F, Serek-Heuberger J, Coles M, Hartmann MD, Habeck M, Martin J, Lupas AN, Alva V
J Mol Biol 427 910-923 (2015)
PMID: 25576874

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 10.06 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32795 (Residues: 97-176; Coverage: 11%)
Gene names: OSD1, YME1, YP9367.04, YPR024W, YTA11
Sequence domains: Yme1-like, N-terminal

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing, NOESY back-calculation
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Metalloproteases of the Inner Mitochondrial Membrane.
Levytskyy et al. (2017)
4 more

1 mention without citation

Multifunctional Mitochondrial AAA Proteases.
Glynn SE. (2017)