› 5glg

X-ray diffraction
1.8Å resolution

The novel function of Osm1 under anaerobic condition in the ER was revealed by crystal structure of Osm1, a soluble fumarate reductase in yeast

Released:
DOI: 10.2210/pdb5glg/pdb
PDB entry 5glg coloured by chain, front view.
PDB entry 5glg coloured by chain, side view.
PDB entry 5glg coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase.
Kim S, Kim CM, Son YJ, Choi JY, Siegenthaler RK, Lee Y, Jang TH, Song J, Kang H, Kaiser CA, Park HH
Nat Commun 9 4867 (2018)
PMID: 30451826

Function and Biology Details

Reaction catalysed: 
Succinate + NAD(+) = fumarate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149225 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarate reductase 2 Chain: A
Molecule details ›
Chain: A
Length: 471 amino acids
Theoretical weight: 51.6 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P21375 (Residues: 32-501; Coverage: 94%)
Gene names: J1659, OSM1, YJR051W
Sequence domains: FAD binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand SIN 1 x SIN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21
Unit cell:
a: 43.638Å b: 109.274Å c: 49.933Å
α: 90° β: 112.55° γ: 90°
R-values:
R R work R free
0.181 0.179 0.214
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Advanced Strategies for Production of Natural Products in Yeast.
Chen et al. (2020)
1 more

4 mentions without citation

An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond.
Iverson et al. (2023)
3 more