5kyo: Difference between revisions
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New page: '''Unreleased structure''' The entry 5kyo is ON HOLD Authors: Birgit Unterweger, Nyssa Drinkwater, Geoffrey J.Dumsday, Sheena McGowan Description: Crystal Structure of CYP101J2 [[Categ... |
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The | ==Crystal Structure of CYP101J2== | ||
<StructureSection load='5kyo' size='340' side='right'caption='[[5kyo]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5kyo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_yanoikuyae Sphingobium yanoikuyae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KYO 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=5kyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kyo OCA], [https://pdbe.org/5kyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kyo RCSB], [https://www.ebi.ac.uk/pdbsum/5kyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kyo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1C9CIU0_SPHYA A0A1C9CIU0_SPHYA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cytochrome P450 monooxygenases (P450s) catalyse a vast array of oxygenation reactions that can be useful in biocatalytic applications. CYP101J2 from Sphingobium yanoikuyae is a P450 that catalyses the hydroxylation of 1,8-cineole. Here we report the crystallisation and X-ray structure elucidation of recombinant CYP101J2 to 1.8 A resolution. The CYP101J2 structure shows the canonical P450-fold and has an open conformation in the absence of substrate. Analysis of the structure revealed that CYP101J2, in the absence of substrate, forms a well-ordered substrate-binding channel that suggests a unique form of substrate guidance in comparison to other bacterial 1,8-cineole-hydroxylating P450 enzymes. This article is protected by copyright. All rights reserved. | |||
X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.,Unterweger B, Drinkwater N, Johanesen P, Lyras D, Dumsday GJ, McGowan S Proteins. 2016 Dec 9. doi: 10.1002/prot.25227. PMID:27936485<ref>PMID:27936485</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5kyo" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sphingobium yanoikuyae]] | |||
[[Category: Drinkwater N]] | |||
[[Category: Dumsday GJ]] | |||
[[Category: McGowan S]] | |||
[[Category: Unterweger B]] | |||
Latest revision as of 15:45, 4 October 2023
Crystal Structure of CYP101J2Crystal Structure of CYP101J2
Structural highlights
FunctionPublication Abstract from PubMedThe cytochrome P450 monooxygenases (P450s) catalyse a vast array of oxygenation reactions that can be useful in biocatalytic applications. CYP101J2 from Sphingobium yanoikuyae is a P450 that catalyses the hydroxylation of 1,8-cineole. Here we report the crystallisation and X-ray structure elucidation of recombinant CYP101J2 to 1.8 A resolution. The CYP101J2 structure shows the canonical P450-fold and has an open conformation in the absence of substrate. Analysis of the structure revealed that CYP101J2, in the absence of substrate, forms a well-ordered substrate-binding channel that suggests a unique form of substrate guidance in comparison to other bacterial 1,8-cineole-hydroxylating P450 enzymes. This article is protected by copyright. All rights reserved. X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.,Unterweger B, Drinkwater N, Johanesen P, Lyras D, Dumsday GJ, McGowan S Proteins. 2016 Dec 9. doi: 10.1002/prot.25227. PMID:27936485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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