3OFT

Crystal Structure of Cytochrome P450 CYP101C1

Summary for 3OFT

• Entry DOI: 10.2210/pdb3oft/pdb
• Related: 3OFU
• Descriptor: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, (2R,5R)-hexane-2,5-diol, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Novosphingobium aromaticivorans
• Total number of polymer chains: 3
• Total formula weight: 133308.32

Authors

Zhou, W.,Ma, M.,Bell, S.G.,Yang, W.,Hao, Y.,Rees, N.H.,Bartlam, M.,Wong, L.-L.,Rao, Z. (deposition date: 2010-08-16, release date: 2011-07-20, Last modification date: 2023-11-01)

Primary citation

Ma, M.,Bell, S.G.,Yang, W.,Hao, Y.,Rees, N.H.,Bartlam, M.,Zhou, W.,Wong, L.L.,Rao, Z.
Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.
Chembiochem, 12:88-99, 2011

PubMed Abstract: CYP101C1 from Novosphingobium aromaticivorans DSM12444 is a homologue of CYP101D1 and CYP101D2 enzymes from the same bacterium and CYP101A1 from Pseudomonas putida. CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives including α- and β-ionone and β-damascone. The activity of CYP101C1 was highest with β-damascone (k(cat)=86 s(-1)) but α-ionone oxidation was the most regioselective (98 % at C3). The crystal structures of hexane-2,5-diol- and β-ionone-bound CYP101C1 have been solved; both have open conformations and the hexanediol-bound form has a clear access channel from the heme to the bulk solvent. The entrance of this channel is blocked when β-ionone binds to the enzyme. The heme moiety of CYP101C1 is in a significantly different environment compared to the other structurally characterised CYP101 enzymes. The likely ferredoxin binding site on the proximal face of CYP101C1 has a different topology but a similar overall positive charge compared to CYP101D1 and CYP101D2, all of which accept electrons from the ArR/Arx class I electron transfer system.

PubMed: 21154803
DOI: 10.1002/cbic.201000537

Experimental method

X-RAY DIFFRACTION (1.9 Å)