Comment
doi: 10.1126/science.1069823.
Enzymology. A moving story
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- PMID: 11859184
- PMCID: PMC3907122
- DOI: 10.1126/science.1069823
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Comment
Enzymology. A moving story
Science.
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No abstract available
Figures
Space-filling atomic structure of the complex between the enzyme cyclophilin A and its substrate cis-Suc-Ala-Phe-Pro-4-NA (20). The substrate is green; residues whose backbone amides detect motional changes due to repetitive substrate binding and dissociation are blue. The catalytic residue arginine 55 is shown in yellow. This residue forms a hydrogen bond to the substrate and detects a motional frequency similar to the catalytic rate, suggesting that it could be involved in motions leading to the formation and decay of the transition state.
Comment on
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Enzyme dynamics during catalysis.Science. 2002 Feb 22;295(5559):1520-3. doi: 10.1126/science.1066176. Science. 2002. PMID: 11859194
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