4yt3: Difference between revisions

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'''Unreleased structure'''


The entry 4yt3 is ON HOLD until Paper Publication
==CYP106A2==
<StructureSection load='4yt3' size='340' side='right' caption='[[4yt3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yt3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YT3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xzo|4xzo]]</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=4yt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yt3 OCA], [http://pdbe.org/4yt3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yt3 RCSB], [http://www.ebi.ac.uk/pdbsum/4yt3 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CPXM_BACME CPXM_BACME]] Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.<ref>PMID:18481342</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CYP106A2 from Bacillus megaterium ATCC 13368 is known as a bacterial steroid hydroxylase which is also capable to hydroxylate a variety of terpenoids. To further analyze the substrate specificity of this enzyme, different resin acids of the abietane- and pimarane-type were tested towards binding and conversion. Product formation could be shown for all tested substrates. Spectroscopic studies revealed type-I binding spectra for isopimaric acid but dehydroabietic acid did not induce a high-spin shift of the enzyme. Interestingly, binding of abietic acid resulted in a type-II difference spectrum typical for nitrogenous inhibitors. Co-crystallization of CYP106A2 with abietic acid and structure determination revealed a bending of the heme-cofactor when abietic acid was bound in the active site. Quantum chemical calculations strongly suggest that this heme distortion is the cause of the unusual spectroscopic characteristics.


Authors: janocha, S., carius, y., bernhardt, r., lancaster, c.r.d.
Crystal structure of CYP106A2 in substrate-free and substrate-bound form.,Janocha S, Carius Y, Hutter M, Lancaster CR, Bernhardt R Chembiochem. 2016 Feb 11. doi: 10.1002/cbic.201500524. PMID:26864272<ref>PMID:26864272</ref>


Description: CYP106A2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Lancaster, C.R.D]]
<div class="pdbe-citations 4yt3" style="background-color:#fffaf0;"></div>
[[Category: Carius, Y]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bernhardt, r]]
[[Category: Carius, y]]
[[Category: Janocha, S]]
[[Category: Janocha, S]]
[[Category: Bernhardt, R]]
[[Category: Lancaster, c r.d]]
[[Category: 15-beta-hydroxylase]]
[[Category: Cytochrome p450]]
[[Category: Mono-oxygenase]]
[[Category: Oxidoreductase]]
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