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The dynamics of camphor in the cytochrome P450 CYP101D2.

Abstract:

The recent crystal structures of CYP101D2, a cytochrome P450 protein from the oligotrophic bacterium Novosphingobium aromaticivorans DSM12444 revealed that both the native (substrate-free) and camphor-soaked forms have open conformations. Furthermore, two other potential camphor-binding sites were also identified from electron densities in the camphor-soaked structure, one being located in the access channel and the other in a cavity on the surface near the F-helix side of the F-G loop termed...

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Publication status:
Published

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Publisher copy:
10.1002/pro.2309

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Journal:
Protein science : a publication of the Protein Society More from this journal
Volume:
22
Issue:
9
Pages:
1218-1229
Publication date:
2013-09-01
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
Language:
English
Keywords:
Pubs id:
pubs:410918
UUID:
uuid:638f8316-9dcc-4629-b19f-0c975a9472f2
Local pid:
pubs:410918
Source identifiers:
410918
Deposit date:
2013-11-17

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