1r30
From Proteopedia
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. 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 Sat May 3 07:00:50 2008
