2VE4
Substrate free cyanobacterial CYP120A1
Summary for 2VE4
| Entry DOI | 10.2210/pdb2ve4/pdb |
| Related | 2VE3 |
| Descriptor | PUTATIVE CYTOCHROME P450 120, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | oxidoreductase, monooxygenase, metal-binding, heme, iron |
| Biological source | SYNECHOCYSTIS SP. |
| Total number of polymer chains | 2 |
| Total formula weight | 102499.23 |
| Authors | Kuhnel, K.,Ke, N.,Sligar, S.G.,Schuler, M.A.,Schlichting, I. (deposition date: 2007-10-16, release date: 2008-04-29, Last modification date: 2024-05-08) |
| Primary citation | Kuhnel, K.,Ke, N.,Cryle, M.J.,Sligar, S.G.,Schuler, M.A.,Schlichting, I. Crystal Structures of Substrate-Free and Retinoic Acid-Bound Cyanobacterial Cytochrome P450 Cyp120A1. Biochemistry, 47:6552-, 2008 Cited by PubMed Abstract: The crystal structures of substrate-free and all-trans-retinoic acid-bound CYP120A1 from Synechocystis sp. PCC 6803 were determined at 2.4 and 2.1 A resolution, respectively, representing the first structural characterization of a cyanobacterial P450. Features of CYP120A1 not observed in other P450 structures include an aromatic ladder flanking the channel leading to the active site and a triple-glycine motif within SRS5. Using spectroscopic methods, CYP120A1 is shown to bind 13-cis-retinoic acid, 9-cis-retinoic acid, and retinal with high affinity and dissociation constants of less than 1 microM. Metabolism of retinoic acid by CYP120A1 suggests that CYP120A1 hydroxylates a variety of retinoid derivatives in vivo. On the basis of the retinoic acid-bound CYP120A1 crystal structure, we propose that either carbon 2 or the methyl groups (C16 or C17) of the beta-ionone ring are modified by CYP120A1. PubMed: 18512957DOI: 10.1021/BI800328S PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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