8gtl
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Cytochrome P450 (CYP101D5)== | |
| + | <StructureSection load='8gtl' size='340' side='right'caption='[[8gtl]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gtl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_echinoides Sphingomonas echinoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GTL FirstGlance]. <br> | ||
| + | </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=8gtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gtl OCA], [https://pdbe.org/8gtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gtl RCSB], [https://www.ebi.ac.uk/pdbsum/8gtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gtl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytochrome P450 enzymes (CYPs) are heme-containing enzymes that catalyze hydroxylation with a variety of biological molecules. Despite their diverse activity and substrates, the structures of CYPs are limited to a tertiary structure that is similar across all the enzymes. It has been presumed that CYPs overcome substrate selectivity with highly flexible loops and divergent sequences around the substrate entrance region. Here, we report the newly identified CYP101D5 from Sphingomonas echinoides. CYP101D5 catalyzes the hydroxylation of beta-ionone and flavonoids, including naringenin and apigenin, and causes the dehydrogenation of alpha-ionone. A structural investigation and comparison with other CYP101 families indicated that spatial constraints at the substrate-recognition site originate from the B/C loop. Furthermore, charge distribution at the substrate binding site may be important for substrate selectivity and the preference for CYP101D5. | ||
| - | + | Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides.,Subedi P, Do H, Lee JH, Oh TJ Int J Mol Sci. 2022 Nov 1;23(21):13317. doi: 10.3390/ijms232113317. PMID:36362105<ref>PMID:36362105</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8gtl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sphingomonas echinoides]] | ||
| + | [[Category: Do H]] | ||
| + | [[Category: Lee JH]] | ||
Revision as of 09:12, 28 December 2022
Crystal Structure of Cytochrome P450 (CYP101D5)
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