View source for 5iqu


==WelO5 G166D variant bound to Fe(II), 2-oxoglutarate, and 12-epifischerindole U==
<StructureSection load='5iqu' size='340' side='right'caption='[[5iqu]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iqu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hapalosiphon_welwitschii_UTEX_B_1830 Hapalosiphon welwitschii UTEX B 1830]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IQU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6CU:(6AS,9R,10R,10AS)-9-ETHYL-10-ISOCYANO-6,6,9-TRIMETHYL-5,6,6A,7,8,9,10,10A-OCTAHYDROINDENO[2,1-B]INDOLE'>6CU</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5iqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqu OCA], [https://pdbe.org/5iqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iqu RCSB], [https://www.ebi.ac.uk/pdbsum/5iqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A067YX61_9CYAN A0A067YX61_9CYAN] 
<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 5iqu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Hapalosiphon welwitschii UTEX B 1830]]
[[Category: Large Structures]]
[[Category: Boal AK]]
[[Category: Maggiolo AO]]
[[Category: Mitchell AJ]]