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1r30

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{{STRUCTURE_1r30| PDB=1r30 | SCENE= }}
{{STRUCTURE_1r30| PDB=1r30 | SCENE= }}
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'''The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme'''
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===The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14704425 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14704425}}
==About this Structure==
==About this Structure==
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[[Category: Sam radical protein]]
[[Category: Sam radical protein]]
[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:59:40 2008''

Revision as of 07:59, 29 July 2008

Image:1r30.png

Template:STRUCTURE 1r30

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

Template:ABSTRACT PUBMED 14704425

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 Tue Jul 29 10:59:40 2008

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