6b86: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6b86' size='340' side='right' caption='[[6b86]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='6b86' size='340' side='right' caption='[[6b86]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6b86]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B86 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6b86]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neucr Neucr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B86 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cao-1, NCU07008 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367110 NEUCR])</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=6b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b86 OCA], [http://pdbe.org/6b86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b86 RCSB], [http://www.ebi.ac.uk/pdbsum/6b86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b86 ProSAT]</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=6b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b86 OCA], [http://pdbe.org/6b86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b86 RCSB], [http://www.ebi.ac.uk/pdbsum/6b86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carotenoid cleavage oxygenases (CCO) are non-heme iron enzymes that catalyze oxidative cleavage of alkene bonds in carotenoid and stilbenoid substrates. Previously, we showed that the iron cofactor of CAO1, a resveratrol-cleaving member of this family, can be substituted with cobalt to yield a catalytically inert enzyme useful for trapping active site-bound stilbenoid substrates for structural characterization. Metal substitution may provide a general method for identifying the natural substrates for CCOs in addition to facilitating structural and biophysical characterization of CCO-carotenoid complexes under normal aerobic conditions. Here, we demonstrate the general applicability of cobalt substitution in a prototypical carotenoid cleaving CCO, apocarotenoid oxygenase (ACO) from Synechocystis. Among the non-native divalent metals investigated, cobalt was uniquely able to stably occupy the ACO metal binding site and inhibit catalysis. Analysis by X-ray crystallography and X-ray absorption spectroscopy demonstrate that the Co(II) forms of both ACO and CAO1 exhibit a close structural correspondence to the native Fe(II) enzyme forms. Hence, cobalt substitution is an effective strategy for generating catalytically inert but structurally intact forms of CCOs. | |||
Preparation and characterization of metal-substituted carotenoid cleavage oxygenases.,Sui X, Farquhar ER, Hill HE, von Lintig J, Shi W, Kiser PD J Biol Inorg Chem. 2018 Aug;23(6):887-901. doi: 10.1007/s00775-018-1586-0. Epub, 2018 Jun 26. PMID:29946976<ref>PMID:29946976</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6b86" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Neucr]] | |||
[[Category: Hill, H E]] | [[Category: Hill, H E]] | ||
[[Category: Kiser, P D]] | [[Category: Kiser, P D]] | ||
Revision as of 12:28, 16 January 2019
2.2A Crystal Structure of Co-CAO1
| ||||||||||||
