Structural highlights
FunctionPublication Abstract from PubMedCYP101D2 from Novosphingobium aromaticivorans DSM12444 is closely related to CYP101D1 from the same bacterium and to P450cam (CYP101A1) from Pseudomonas putida. All three are capable of oxidising camphor stereoselectively to 5-exo-hydroxycamphor. The crystal structure of CYP101D2 reveals that the likely ferredoxin binding site on the proximal face is largely positively charged, similar to that of CYP101D1. However, both the native and camphor-soaked forms of CYP101D2 have open conformations with an access channel. In the active site of the camphor-soaked form the camphor carbonyl interacts with the heme iron-bound water. Two other potential camphor binding sites were also identified from electron densities in the camphor-soaked structure: one is located in the access channel, flanked by the B/C and F/G loops and the I helix, and the other in a cavity on the surface of the enzyme near the F helix side of the F/G loop. The observed open structures may be conformers of the CYP101D2 enzyme which enable the substrate to enter the buried active site via a conformational selection mechanism. The second and third binding sites may be intermediate locations of substrate entry and translocation into the active site, and provide insight into a multi-step substrate binding mechanism. The structure of CYP101D2 unveils a potential path for substrate entry into the active site.,Yang W, Bell SG, Wang H, Zhou W, Bartlam M, Wong LL, Rao Z Biochem J. 2010 Oct 15. PMID:20950270[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
This page was last modified 16:51, 1 November 2023.