1R30

The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme

Summary for 1R30

• Entry DOI: 10.2210/pdb1r30/pdb
• Descriptor: Biotin synthase, S-ADENOSYLMETHIONINE, IRON/SULFUR CLUSTER, ... (6 entities in total)
• Functional Keywords: sam radical protein, tim barrel, fes cluster, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 85127.86

Authors

Berkovitch, F.,Nicolet, Y.,Wan, J.T.,Jarrett, J.T.,Drennan, C.L. (deposition date: 2003-09-30, release date: 2004-01-13, Last modification date: 2024-02-14)

Primary citation

Berkovitch, F.,Nicolet, Y.,Wan, J.T.,Jarrett, J.T.,Drennan, C.L.
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.
Science, 303:76-79, 2004

PubMed Abstract: 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.

PubMed: 14704425
DOI: 10.1126/science.1088493

Experimental method

X-RAY DIFFRACTION (3.4 Å)