4z82: Difference between revisions
New page: '''Unreleased structure''' The entry 4z82 is ON HOLD until Paper Publication Authors: Fellner, M., Tchesnokov, E.P., Siakkou, E., Rutledge, M.T., Kanitz, M., Jameson, G.N.L., Wilbanks, ... |
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==Cysteine bound rat cysteine dioxygenase C164S variant at pH 8.1== | |||
<StructureSection load='4z82' size='340' side='right'caption='[[4z82]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4z82]] 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=4Z82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z82 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</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=4z82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z82 OCA], [https://pdbe.org/4z82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z82 RCSB], [https://www.ebi.ac.uk/pdbsum/4z82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z82 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CDO1_RAT CDO1_RAT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cysteine dioxygenase is a non-heme mononuclear iron enzyme with unique structural features, namely an intramolecular thioether cross-link between cysteine 93 and tyrosine 157, and a disulfide bond between substrate L-cysteine and cysteine 164 in the entrance channel to the active site. We investigated how these posttranslational modifications affect catalysis through a kinetic, crystallographic and computational study. The enzyme kinetics of a C164S variant are identical to WT, indicating that disulfide formation at C164 does not significantly impair access to the active site at physiological pH. However, at high pH, the cysteine-tyrosine cross-link formation is enhanced in C164S. This supports the view that disulfide formation at position 164 can limit access to the active site. The C164S variant yielded crystal structures of unusual clarity in both resting state and with cysteine bound. Both show that the iron in the cysteine-bound complex is a mixture of penta- and hexa-coordinate with a water molecule taking up the final site (60 % occupancy), which is where dioxygen is believed to coordinate during turnover. The serine also displays stronger hydrogen bond interactions to a water bound to the amine of the substrate cysteine. However, the interactions between cysteine and iron appear unchanged. DFT calculations support this and show that WT and C164S have similar binding energies for the water molecule in the final site. This variant therefore provides evidence that WT also exists in an equilibrium between penta- and hexa-coordinate forms and the presence of the sixth ligand does not strongly affect dioxygen binding. | |||
Influence of cysteine 164 on active site structure in rat cysteine dioxygenase.,Fellner M, Siakkou E, Faponle AS, Tchesnokov EP, de Visser SP, Wilbanks SM, Jameson GN J Biol Inorg Chem. 2016 May 18. PMID:27193596<ref>PMID:27193596</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4z82" style="background-color:#fffaf0;"></div> | ||
[[Category: Fellner | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Wilbanks | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Fellner M]] | |||
[[Category: Jameson GNL]] | |||
[[Category: Kanitz M]] | |||
[[Category: Rutledge MT]] | |||
[[Category: Siakkou E]] | |||
[[Category: Tchesnokov EP]] | |||
[[Category: Wilbanks SM]] | |||
Latest revision as of 11:13, 27 September 2023
Cysteine bound rat cysteine dioxygenase C164S variant at pH 8.1Cysteine bound rat cysteine dioxygenase C164S variant at pH 8.1
Structural highlights
FunctionPublication Abstract from PubMedCysteine dioxygenase is a non-heme mononuclear iron enzyme with unique structural features, namely an intramolecular thioether cross-link between cysteine 93 and tyrosine 157, and a disulfide bond between substrate L-cysteine and cysteine 164 in the entrance channel to the active site. We investigated how these posttranslational modifications affect catalysis through a kinetic, crystallographic and computational study. The enzyme kinetics of a C164S variant are identical to WT, indicating that disulfide formation at C164 does not significantly impair access to the active site at physiological pH. However, at high pH, the cysteine-tyrosine cross-link formation is enhanced in C164S. This supports the view that disulfide formation at position 164 can limit access to the active site. The C164S variant yielded crystal structures of unusual clarity in both resting state and with cysteine bound. Both show that the iron in the cysteine-bound complex is a mixture of penta- and hexa-coordinate with a water molecule taking up the final site (60 % occupancy), which is where dioxygen is believed to coordinate during turnover. The serine also displays stronger hydrogen bond interactions to a water bound to the amine of the substrate cysteine. However, the interactions between cysteine and iron appear unchanged. DFT calculations support this and show that WT and C164S have similar binding energies for the water molecule in the final site. This variant therefore provides evidence that WT also exists in an equilibrium between penta- and hexa-coordinate forms and the presence of the sixth ligand does not strongly affect dioxygen binding. Influence of cysteine 164 on active site structure in rat cysteine dioxygenase.,Fellner M, Siakkou E, Faponle AS, Tchesnokov EP, de Visser SP, Wilbanks SM, Jameson GN J Biol Inorg Chem. 2016 May 18. PMID:27193596[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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