› 2xcz

X-ray diffraction
1.64Å resolution

Crystal Structure of macrophage migration inhibitory factor homologue from Prochlorococcus marinus

Released:
DOI: 10.2210/pdb2xcz/pdb
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Source organism: Prochlorococcus marinus str. MIT 9313
Primary publication:
Structural and functional characterization of a macrophage migration inhibitory factor homologue from the marine cyanobacterium Prochlorococcus marinus .
Wasiel AA, Rozeboom HJ, Hauke D, Baas BJ, Zandvoort E, Quax WJ, Thunnissen AM, Poelarends GJ
Biochemistry 49 7572-81 (2010)
PMID: 20715791

Function and Biology Details

Reactions catalysed: 
Keto-phenylpyruvate = enol-phenylpyruvate
L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182059 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-dopachrome isomerase Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 12.38 KDa
Source organism: Prochlorococcus marinus str. MIT 9313
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7V867 (Residues: 1-115; Coverage: 100%)
Gene name: PMT_0503
Sequence domains: Macrophage migration inhibitory factor (MIF)
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

1 bound ligand:
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P63
Unit cell:
a: 52.45Å b: 52.45Å c: 63.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.164 0.213
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

The non-mammalian MIF superfamily.
Sparkes et al. (2017)
4 more

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