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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

Authors


Johnson, EO More by this author
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Journal:
Dalton transactions (Cambridge, England : 2003)
Volume:
41
Issue:
28
Pages:
8703-8714
Publication date:
2012-07-05
DOI:
EISSN:
1477-9234
ISSN:
1477-9226
URN:
uuid:839c3c62-a249-4158-a27e-ae759a2e668f
Source identifiers:
339838
Local pid:
pubs:339838

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