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InterPro: IPR018506 Cytochrome b5, heme-binding site
Protein matches
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UniProtKB Matches: 1405 proteins |
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Accession
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IPR018506 Cyt_B5_heme-BS |
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Type
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Binding_site |
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Signatures
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InterPro Relationships
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Found in
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IPR001199 Cytochrome b5
IPR009160 Delta-9 acyl-CoA desaturase, haem/steroid binding region-containing
IPR012137 Nitrate reductase NADH dependent
IPR014430 Inositolphosphorylceramide-B hydroxylase
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GO Term annotation
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Function
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GO:0020037 heme binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Cytochromes b5 are ubiquitous electron transport proteins found in animals, plants and
yeasts [1]. The microsomal and mitochondrial variants are membrane-bound,
while those from erythrocytes and other animal tissues are water-soluble [2, 3]. The 3D structure of bovine cyt b5 is known, the
fold belonging to the alpha+beta class, with 5 strands and 5 short helices
forming a framework for supporting a central haem group [4]. The cytochrome b5 domain is similar to that of a number
of oxidoreductases, such as plant and fungal nitrate reductases, sulphite oxidase, yeast
flavocytochrome b2 (L-lactate dehydrogenase) and plant cyt b5/acyl lipid desaturase
fusion protein.
This conserved site includes the first of the two histidine heme ligands, which are found in the heme-binding domain of cytochrome b5 family.
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Structural links
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Additional Reading
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Mowat CG, Wehenkel A, Green AJ, Walkinshaw MD, Reid GA, Chapman SK.
Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation.
Biochemistry 43 2004 9519-26
[PubMed: 15260495]
http://dx.doi.org/10.1021/bi049263m
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Levin RJ, Boychuk PL, Croniger CM, Kazzaz JA, Rozek CE.
Structure and expression of a muscle specific gene which is adjacent to the Drosophila myosin heavy-chain gene and can encode a cytochrome b related protein.
Nucleic Acids Res. 17 1989 6349-67
[PubMed: 2549511]
http://dx.doi.org/10.1093/nar/17.15.6349
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Guiard B.
Structure, expression and regulation of a nuclear gene encoding a mitochondrial protein: the yeast L(+)-lactate cytochrome c oxidoreductase (cytochrome b2).
EMBO J. 4 1985 3265-72
[PubMed: 3004948]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=3004948&action=stream&blobtype=pdf
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Wang L, Sun N, Terzyan S, Zhang X, Benson DR.
A histidine/tryptophan pi-stacking interaction stabilizes the heme-independent folding core of microsomal apocytochrome b5 relative to that of mitochondrial apocytochrome b5.
Biochemistry 45 2006 13750-9
[PubMed: 17105194]
http://dx.doi.org/10.1021/bi0615689
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Shan L, Lu JX, Gan JH, Wang YH, Huang ZX, Xia ZX.
Structure of the F58W mutant of cytochrome b5: the mutation leads to multiple conformations and weakens stacking interactions.
Acta Crystallogr. D Biol. Crystallogr. 61 2005 180-9
[PubMed: 15681869]
http://dx.doi.org/10.1107/S0907444904031798
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Wang L, Cowley AB, Terzyan S, Zhang X, Benson DR.
Comparison of cytochromes b5 from insects and vertebrates.
Proteins 67 2007 293-304
[PubMed: 17299762]
http://dx.doi.org/10.1002/prot.21250
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Tsai CL, Gokulan K, Sobrado P, Sacchettini JC, Fitzpatrick PF.
Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base.
Biochemistry 46 2007 7844-51
[PubMed: 17563122]
http://dx.doi.org/10.1021/bi7005543
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Crawford NM, Smith M, Bellissimo D, Davis RW.
Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains.
Proc. Natl. Acad. Sci. U.S.A. 85 1988 5006-10
[PubMed: 3393528]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=3393528&action=stream&blobtype=pdf
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Guiard B, Lederer F.
Amino acid sequence of the 'b5-like' heme-binding domain from chicken sulfite oxidase.
Eur. J. Biochem. 100 1979 441-53
[PubMed: 510290]
http://dx.doi.org/10.1111/j.1432-1033.1979.tb04187.x
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InterPro 23.1
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