View source for 9cjg


==P450-G9 from Actinokineospora terrae, a non-canonical, serine-ligated cytochrome P450 in the ligand-free, closed conformation==
<StructureSection load='9cjg' size='340' side='right'caption='[[9cjg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cjg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudonocardiaceae Pseudonocardiaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CJG 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BO:1-BUTANOL'>1BO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <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=9cjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cjg OCA], [https://pdbe.org/9cjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cjg RCSB], [https://www.ebi.ac.uk/pdbsum/9cjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cjg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1H9KM06_9PSEU A0A1H9KM06_9PSEU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome P450s (CYPs) are a superfamily of thiolate-ligated heme metalloenzymes principally responsible for the hydroxylation of unactivated C-H bonds. The lower-axial cysteine is an obligatory and universally conserved residue for the CYP enzyme class. Herein, we challenge this paradigm by systematically identifying non-canonical CYPs (ncCYPs) that do not harbor a cysteine ligand. Our bioinformatic search reveals 20 distinct ncCYP families with diverse ligands encoded in microbial genomes. We characterize a native serine-ligated CYP with a high-spin ferric resting state. Its crystal structure clearly shows a typical CYP fold and a serine alkoxide as a lower axial heme ligand. In addition, we report the discovery and characterization of the first native selenocysteine-ligated CYP in nature. Our findings radically expand the CYP metalloenzyme family.

Non-Canonical Cytochrome P450 Enzymes in Nature.,Nguy AKL, Ireland KA, Kayrouz CM, Caceres JC, Greene BL, Davis KM, Seyedsayamdost MR bioRxiv [Preprint]. 2024 Dec 23:2024.12.22.630014. doi: , 10.1101/2024.12.22.630014. PMID:39763895<ref>PMID:39763895</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cjg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudonocardiaceae]]
[[Category: Davis KM]]
[[Category: Ireland KA]]