7q9e: Difference between revisions
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==CYP106A1== | |||
<StructureSection load='7q9e' size='340' side='right'caption='[[7q9e]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7q9e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_DSM_319 Priestia megaterium DSM 319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q9E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7q9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q9e OCA], [https://pdbe.org/7q9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q9e RCSB], [https://www.ebi.ac.uk/pdbsum/7q9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q9e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D5DF35_PRIM3 D5DF35_PRIM3] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Understanding the structural basis of the selectivity of steroid hydroxylation requires detailed structural and functional investigations on various steroid hydroxylases with different selectivities, such as the bacterial cytochrome P450 enzymes. Here, the crystal structure of the cytochrome P450 CYP106A1 from Priestia megaterium was solved. CYP106A1 exhibits a rare additional structural motif of a cytochrome P450, a sixth beta-sheet. The protein was found in different unusual conformations corresponding to both open and closed forms even when crystallized without any known substrate. The structural comparison of CYP106A1 with the previously investigated CYP106A2, including docking studies for both isoforms with the substrate cortisol, reveals a completely different orientation of the steroid molecule in the active sites. This distinction convincingly explains the experimentally observed differences in substrate conversion and product formation by the two enzymes. | |||
Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion.,Carius Y, Hutter M, Kiss F, Bernhardt R, Lancaster CRD FEBS Lett. 2022 Sep 23. doi: 10.1002/1873-3468.14502. PMID:36151590<ref>PMID:36151590</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7q9e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Priestia megaterium DSM 319]] | |||
[[Category: Bernhardt R]] | |||
[[Category: Carius Y]] | |||
[[Category: Hutter M]] | |||
[[Category: Kiss F]] | |||
[[Category: Lancaster CRD]] | |||
Revision as of 22:18, 19 October 2022
CYP106A1CYP106A1
Structural highlights
FunctionPublication Abstract from PubMedUnderstanding the structural basis of the selectivity of steroid hydroxylation requires detailed structural and functional investigations on various steroid hydroxylases with different selectivities, such as the bacterial cytochrome P450 enzymes. Here, the crystal structure of the cytochrome P450 CYP106A1 from Priestia megaterium was solved. CYP106A1 exhibits a rare additional structural motif of a cytochrome P450, a sixth beta-sheet. The protein was found in different unusual conformations corresponding to both open and closed forms even when crystallized without any known substrate. The structural comparison of CYP106A1 with the previously investigated CYP106A2, including docking studies for both isoforms with the substrate cortisol, reveals a completely different orientation of the steroid molecule in the active sites. This distinction convincingly explains the experimentally observed differences in substrate conversion and product formation by the two enzymes. Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion.,Carius Y, Hutter M, Kiss F, Bernhardt R, Lancaster CRD FEBS Lett. 2022 Sep 23. doi: 10.1002/1873-3468.14502. PMID:36151590[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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