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A Role for the Strained Phenylalanine Ring Rotation Induced by Substrate Binding to Cytochrome CYP102A1

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X-ray crystal structures of CYP102A1 (P450BM-3) have shown that PHE87 rotates upon substrate binding and is in contact with the heme cofactor. Analysis of substrate binding data combined with DFT calculations suggest that the ring is rotated into an unfavorable interaction with the heme and this could drive active site rearrangement.

Keywords: Cytochrome P450; DFT; actuation; protein dynamics; protein structure; substrate binding

Document Type: Research Article


Affiliations: Department of Chemistry,University of Texas at Dallas, Box 830688, BE26, Richardson, TX 75083-0688, USA.

Publication date: 2006-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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