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5ul2

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==Structure of Apo, SeMet-labeled Cobalamin-dependent S-adenosylmethionine radical enzyme OxsB==
==Structure of Apo, SeMet-labeled Cobalamin-dependent S-adenosylmethionine radical enzyme OxsB==
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<StructureSection load='5ul2' size='340' side='right' caption='[[5ul2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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<StructureSection load='5ul2' size='340' side='right'caption='[[5ul2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ul2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UL2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ul2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UL2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.552&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ul3|5ul3]], [[5ul4|5ul4]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ul2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul2 OCA], [https://pdbe.org/5ul2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ul2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ul2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul2 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxsB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ul2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul2 OCA], [http://pdbe.org/5ul2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ul2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ul2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul2 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O24770_PRIMG O24770_PRIMG]
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Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2'-deoxyadenosine phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2'. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes.
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A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis.,Bridwell-Rabb J, Zhong A, Sun HG, Drennan CL, Liu HW Nature. 2017 Mar 27. doi: 10.1038/nature21689. PMID:28346939<ref>PMID:28346939</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ul2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14581]]
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[[Category: Large Structures]]
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[[Category: Bridwell-Rabb, J]]
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[[Category: Priestia megaterium]]
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[[Category: Drennan, C L]]
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[[Category: Bridwell-Rabb J]]
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[[Category: Cobalamin]]
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[[Category: Drennan CL]]
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[[Category: Metal binding protein]]
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[[Category: Metalloprotein]]
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[[Category: Oxetanocin]]
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[[Category: Radical sam]]
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[[Category: S-adenosylmethionine]]
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Current revision

Structure of Apo, SeMet-labeled Cobalamin-dependent S-adenosylmethionine radical enzyme OxsB

PDB ID 5ul2

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