4ieu: Difference between revisions
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==Cys-persulfenate bound Cysteine Dioxygenase at pH 7.0 in the presence of Cys== | ==Cys-persulfenate bound Cysteine Dioxygenase at pH 7.0 in the presence of Cys== | ||
<StructureSection load='4ieu' size='340' side='right' caption='[[4ieu]], [[Resolution|resolution]] 1.25Å' scene=''> | <StructureSection load='4ieu' size='340' side='right'caption='[[4ieu]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ieu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ieu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IEU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CO:S-HYDROPEROXYCYSTEINE'>2CO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CO:S-HYDROPEROXYCYSTEINE'>2CO</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=4ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ieu OCA], [https://pdbe.org/4ieu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ieu RCSB], [https://www.ebi.ac.uk/pdbsum/4ieu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ieu ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CDO1_RAT CDO1_RAT] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Dioxygenase|Dioxygenase]] | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: Cooley | [[Category: Cooley RB]] | ||
[[Category: Driggers | [[Category: Driggers CM]] | ||
[[Category: Karplus | [[Category: Karplus PA]] | ||
Revision as of 12:05, 9 November 2022
Cys-persulfenate bound Cysteine Dioxygenase at pH 7.0 in the presence of CysCys-persulfenate bound Cysteine Dioxygenase at pH 7.0 in the presence of Cys
Structural highlights
FunctionPublication Abstract from PubMedMammalian cysteine dioxygenase (CDO) is a mononuclear non-heme iron protein that catalyzes the conversion of cysteine (Cys) to cysteine sulfinic acid by an unclarified mechanism. One structural study revealed that a Cys-persulfenate (or Cys-persulfenic acid) formed in the active site, but quantum mechanical calculations have been used to support arguments that it is not an energetically feasible reaction intermediate. Here, we report a series of high-resolution structures of CDO soaked with Cys at pH values from 4 to 9. Cys binding is minimal at pH</=5 and persulfenate formation is consistently seen at pH values between 5.5 and 7. Also, a structure determined using laboratory-based X-ray diffraction shows that the persulfenate, with an apparent average O-O separation distance of ~1.8A, is not an artifact of synchrotron radiation. At pH>/=8, the active-site iron shifts from 4- to 5-coordinate, and Cys soaks reveal a complex with Cys, but no dioxygen, bound. This 'Cys-only' complex differs in detail from a previously published 'Cys-only' complex, which we reevaluate and conclude is not reliable. The high-resolution structures presented here do not resolve the CDO mechanism but do imply that an iron-bound persulfenate (or persulfenic acid) is energetically accessible in the CDO active site, and that CDO active-site chemistry in the crystals is influenced by protonation/deprotonation events with effective pKa values near ~5.5 and ~7.5 that influence Cys binding and oxygen binding/reactivity, respectively. Furthermore, this work provides reliable ligand-bound models for guiding future mechanistic considerations. Cysteine Dioxygenase Structures from pH4 to 9: Consistent Cys-Persulfenate Formation at Intermediate pH and a Cys-Bound Enzyme at Higher pH.,Driggers CM, Cooley RB, Sankaran B, Hirschberger LL, Stipanuk MH, Karplus PA J Mol Biol. 2013 Jun 7. pii: S0022-2836(13)00358-6. doi:, 10.1016/j.jmb.2013.05.028. PMID:23747973[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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