Journal article
The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding site.
- Abstract:
-
The crystal structures of the 4-methoxybenzoate bound forms of cytochrome P450 enzymes CYP199A2 and CYP199A4 from the Rhodopseudomonas palustris strains CGA009 and HaA2 have been solved. The structures of these two enzymes, which share 86% sequence identity, are very similar though some differences are found on the proximal surface. In these structures the enzymes have a closed conformation, in contrast to the substrate-free form of CYP199A2 where an obvious substrate access channel is observ...
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- Publication status:
- Published
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- Publisher copy:
- 10.1039/c2dt30783a
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Authors
Bibliographic Details
- Journal:
- Dalton transactions (Cambridge, England : 2003)
- Volume:
- 41
- Issue:
- 28
- Pages:
- 8703-8714
- Publication date:
- 2012-07-01
- DOI:
- EISSN:
-
1477-9234
- ISSN:
-
1477-9226
- Source identifiers:
-
339838
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:339838
- UUID:
-
uuid:839c3c62-a249-4158-a27e-ae759a2e668f
- Local pid:
- pubs:339838
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2012
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