5iqv: Difference between revisions

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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=5iqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqv OCA], [http://pdbe.org/5iqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqv RCSB], [http://www.ebi.ac.uk/pdbsum/5iqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqv ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

A 2.4-A-resolution X-ray crystal structure of the carrier-protein-independent halogenase WelO5 in complex with its welwitindolinone precursor substrate, 12-epi-fischerindole U, reveals that the C13 chlorination target is proximal to the anticipated site of the oxo group in a presumptive cis-halo-oxo-iron(IV) (haloferryl) intermediate. Prior study of related halogenases forecasts substrate hydroxylation in this active-site configuration, but X-ray crystallographic verification of C13 halogenation in single crystals mandates that ligand dynamics must reposition the oxygen ligand to enable the observed outcome. S189A WelO5 produces a mixture of halogenation and hydroxylation products, showing that an outer-sphere hydrogen-bonding group orchestrates ligand movements to achieve a configuration that promotes halogen transfer.

Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.,Mitchell AJ, Zhu Q, Maggiolo AO, Ananth NR, Hillwig ML, Liu X, Boal AK Nat Chem Biol. 2016 Jun 27. doi: 10.1038/nchembio.2112. PMID:27348090<ref>PMID:27348090</ref>

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

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 8: / Line 8: @@
 <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=5iqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqv OCA], [http://pdbe.org/5iqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqv RCSB], [http://www.ebi.ac.uk/pdbsum/5iqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqv ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A 2.4-A-resolution X-ray crystal structure of the carrier-protein-independent halogenase WelO5 in complex with its welwitindolinone precursor substrate, 12-epi-fischerindole U, reveals that the C13 chlorination target is proximal to the anticipated site of the oxo group in a presumptive cis-halo-oxo-iron(IV) (haloferryl) intermediate. Prior study of related halogenases forecasts substrate hydroxylation in this active-site configuration, but X-ray crystallographic verification of C13 halogenation in single crystals mandates that ligand dynamics must reposition the oxygen ligand to enable the observed outcome. S189A WelO5 produces a mixture of halogenation and hydroxylation products, showing that an outer-sphere hydrogen-bonding group orchestrates ligand movements to achieve a configuration that promotes halogen transfer.
+Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.,Mitchell AJ, Zhu Q, Maggiolo AO, Ananth NR, Hillwig ML, Liu X, Boal AK Nat Chem Biol. 2016 Jun 27. doi: 10.1038/nchembio.2112. PMID:27348090<ref>PMID:27348090</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5iqv" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>