5flj: Difference between revisions
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==enzyme-substrate-dioxygen complex of Ni-quercetinase== | |||
<StructureSection load='5flj' size='340' side='right' caption='[[5flj]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5flj]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FLJ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fle|5fle]], [[5flh|5flh]], [[5fli|5fli]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quercetin_2,3-dioxygenase Quercetin 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.24 1.13.11.24] </span></td></tr> | |||
<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=5flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flj OCA], [http://pdbe.org/5flj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5flj RCSB], [http://www.ebi.ac.uk/pdbsum/5flj PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Quercetin 2,4-dioxygenase (quercetinase) from Streptomyces uses nickel as the active-site cofactor to catalyze oxidative cleavage of the flavonol quercetin. How this unusual active-site metal supports catalysis and O2 activation is under debate. We present crystal structures of Ni-quercetinase in three different states, thus providing direct insight into how quercetin and O2 are activated at the Ni(2+) ion. The Ni(2+) ion is coordinated by three histidine residues and a glutamate residue (E(76) ) in all three states. Upon binding, quercetin replaces one water ligand at Ni and is stabilized by a short hydrogen bond through E(76) , the carboxylate group of which rotates by 90 degrees . This conformational change weakens the interaction between Ni and the remaining water ligand, thereby preparing a coordination site at Ni to bind O2 . O2 binds side-on to the Ni(2+) ion and is perpendicular to the C2-C3 and C3-C4 bonds of quercetin, which are cleaved in the following reaction steps. | |||
Quercetin 2,4-Dioxygenase Activates Dioxygen in a Side-On O2 -Ni Complex.,Jeoung JH, Nianios D, Fetzner S, Dobbek H Angew Chem Int Ed Engl. 2016 Mar 1;55(10):3281-4. doi: 10.1002/anie.201510741., Epub 2016 Feb 5. PMID:26846734<ref>PMID:26846734</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5flj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Quercetin 2,3-dioxygenase]] | |||
[[Category: Dobbek, H]] | [[Category: Dobbek, H]] | ||
[[Category: Fetzner, S]] | |||
[[Category: Jeoung, J H]] | |||
[[Category: Nianios, D]] | [[Category: Nianios, D]] | ||
[[Category: | [[Category: Dioxygen]] | ||
[[Category: | [[Category: Dioxygenase]] | ||
[[Category: Ni-quercetinase]] | |||
[[Category: Nickel]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Streptomyce]] | |||
