1r30
From Proteopedia
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The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
Overview
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.
About this Structure
1R30 is a Single protein structure of sequence from Escherichia coli with SAM, SF4, FES, DTB and TRS as ligands. Active as Biotin synthase, with EC number 2.8.1.6 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 01:13:54 2007
Categories: Biotin synthase | Escherichia coli | Single protein | Berkovitch, F. | Drennan, C.L. | Jarrett, J.T. | Nicolet, Y. | Wan, J.T. | DTB | FES | SAM | SF4 | TRS | Fes cluster | Sam radical protein | Tim barrel
