Structural highlights
1r30 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Gene: | BIOB ("Bacillus coli" Migula 1895) |
| Activity: | Biotin synthase, with EC number 2.8.1.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[BIOB_ECOLI] Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of biotin synthase from Escherichia coli in complex with S-adenosyl-L-methionine and dethiobiotin has been determined to 3.4 angstrom resolution. This structure addresses how "AdoMet radical" or "radical SAM" enzymes use Fe4S4 clusters and S-adenosyl-L-methionine to generate organic radicals. Biotin synthase catalyzes the radical-mediated insertion of sulfur into dethiobiotin to form biotin. The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments.
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.,Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL Science. 2004 Jan 2;303(5654):76-9. PMID:14704425[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sanyal I, Cohen G, Flint DH. Biotin synthase: purification, characterization as a [2Fe-2S]cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry. 1994 Mar 29;33(12):3625-31. PMID:8142361
- ↑ Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science. 2004 Jan 2;303(5654):76-9. PMID:14704425 doi:http://dx.doi.org/10.1126/science.1088493
