The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding site.

Bell, SG; Yang, W; Tan, AB; Zhou, R; Johnson, EO; Zhang, A; Zhou, W; Rao, Z; Wong, LL

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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APA Style

Bell, S. G., Yang, W., Tan, A. B., Zhou, R., Johnson, E. O., Zhang, A., Zhou, W., Rao, Z., & Wong, L. L. (2012). The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding site. Dalton Transactions (Cambridge, England : 2003), 41(28), 8703–8714.

MLA Style

Bell, S. G., et al. “The Crystal Structures of 4-Methoxybenzoate Bound CYP199A2 and CYP199A4: Structural Changes on Substrate Binding and the Identification of an Anion Binding Site.” Dalton Transactions (Cambridge, England : 2003), vol. 41, no. 28, Dalton transactions (Cambridge, England : 2003), 2012, pp. 8703–14.

Chicago Style

Bell, SG, W Yang, AB Tan, R Zhou, EO Johnson, A Zhang, W Zhou, Z Rao, and LL Wong. 2012. “The Crystal Structures of 4-Methoxybenzoate Bound CYP199A2 and CYP199A4: Structural Changes on Substrate Binding and the Identification of an Anion Binding Site.” Dalton Transactions (Cambridge, England : 2003) 41 (28): 8703–14.
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