1r30

<table><tr><td colspan='2'>[[1r30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R30 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R30 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTB:6-(5-METHYL-2-OXO-IMIDAZOLIDIN-4-YL)-HEXANOIC+ACID'>DTB</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biotin_synthase Biotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.6 2.8.1.6] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r30 OCA], [http://pdbe.org/1r30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r30 RCSB], [http://www.ebi.ac.uk/pdbsum/1r30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r30 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BIOB_ECOLI BIOB_ECOLI]] Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.<ref>PMID:8142361</ref>

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== 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<ref>PMID:14704425</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1r30" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Biotin synthase]]

[[Category: Berkovitch, F]]

[[Category: Drennan, C L]]

[[Category: Jarrett, J T]]

[[Category: Nicolet, Y]]

[[Category: Wan, J T]]

[[Category: Transferase]]