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PDBsum entry 6fvh
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PDB id:
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Isomerase
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Title:
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Macrophage migration inhibitory factor (mif) with covalently bound pitc
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Structure:
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Macrophage migration inhibitory factor. Chain: a, b, c. Synonym: mif,glycosylation-inhibiting factor,gif,l-dopachrome isomerase,l-dopachrome tautomerase,phenylpyruvate tautomerase. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mif, glif, mmif. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.40Å
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R-factor:
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0.139
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R-free:
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0.166
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Authors:
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V.R.Samygina,G.Bourenkov,A.V.Sokolov
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Key ref:
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A.V.Sokolov
et al.
(2018).
Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor.
Biochemistry (Mosc),
83,
701-707.
PubMed id:
DOI:
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Date:
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02-Mar-18
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Release date:
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06-Jun-18
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PROCHECK
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Headers
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References
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P14174
(MIF_HUMAN) -
Macrophage migration inhibitory factor from Homo sapiens
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Seq:
Struc:
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115 a.a.
114 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class 2:
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E.C.5.3.2.1
- phenylpyruvate tautomerase.
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Reaction:
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3-phenylpyruvate = enol-phenylpyruvate
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3-phenylpyruvate
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=
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enol-phenylpyruvate
Bound ligand (Het Group name = )
matches with 40.00% similarity
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Enzyme class 3:
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E.C.5.3.3.12
- L-dopachrome isomerase.
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Pathway:
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Reaction:
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L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
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L-dopachrome
Bound ligand (Het Group name = )
matches with 53.33% similarity
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=
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5,6-dihydroxyindole-2-carboxylate
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Cofactor:
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Zn(2+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochemistry (Mosc)
83:701-707
(2018)
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PubMed id:
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Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor.
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A.V.Sokolov,
L.A.Dadinova,
M.V.Petoukhov,
G.Bourenkov,
K.M.Dubova,
S.V.Amarantov,
V.V.Volkov,
V.A.Kostevich,
N.P.Gorbunov,
N.A.Grudinina,
V.B.Vasilyev,
V.R.Samygina.
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ABSTRACT
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Macrophage migration inhibitory factor (MIF) is a key proinflammatory cytokine.
Inhibitors of tautomerase activity of MIF are perspective antiinflammatory
compounds. Ceruloplasmin, the copper-containing ferroxidase of blood plasma, is
a noncompetitive inhibitor of tautomerase activity of MIF in the reaction with
p-hydroxyphenylpyruvate. Small-angle X-ray scattering established a model of the
complex formed by MIF and ceruloplasmin. Crystallographic analysis of MIF with a
modified active site supports the model. The stoichiometry of 3 CP/MIF trimer
complex was established using gel filtration. Conformity of novel data
concerning the interaction regions in the studied proteins with previous
biochemical data is discussed.
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