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. Author manuscript; available in PMC: 2011 Feb 19.
Published in final edited form as: J Mol Biol. 2009 Dec 1;396(2):441–451. doi: 10.1016/j.jmb.2009.11.057

Fig 5. Adaptations for Adrenodoxin Binding.

Fig 5

A) CYP24A1's proximal surface is shown below the heme prosthetic group with key structural elements implicated in adrenodoxin binding noted. Basic residues from helices B, C, D, J, K and L, the Cys-Loop and the (bacterial) meander region line the positively-charged Adx binding. Fully-conserved residues from helices K (K378,K382) and L (R465,R466) known to mediate adrenodoxin binding and electron transfer in related P450s are labeled [52-55]. B) A conserved tryptophan residue (W440), from the K″ helix of mitochondrial P450s, forms a salt-bridge to the K-helix via a fully-conserved glutamate residue (E383) that may contribute to the display of the meander's lysine-rich, proximal loop, that is associated with Adx binding [57]. Residues from the L-helix (R465,R466) and Cys-loop (M462), implicated in the electron shuttle process are shown below the heme in close proximity to the K-helix. The lower portion of the active-site is also shown with CHAPS (pink) positioned above the water (WAT6) bound heme iron.