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Nature 454, 832-833 (14 August 2008) | doi:10.1038/454832a; Published online 13 August 2008
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Assistant Professor and Associate Professor
- Massachusetts General Hospital/ Harvard Medical School
- Charlestown, MA
Faculty - Plant Cellular & Molecular Biology, Molecular Genetics & the Plant Molecular Biology / Biotechnology Program
- The Ohio State University
- Columbus, Ohio
Biochemistry: Fit for an enzyme
Shiven Kapur1 & Chaitan Khosla1
Abstract
Certain enzymes that synthesize antibiotics play a game of pass the parcel, handing biosynthetic intermediates from one active site to another. A study reveals the dynamic nature of interactions between the enzyme domains.
Although crystal structures provide vivid insights into the architecture of enzymes, they reinforce a static picture of the molecules, providing only a snapshot of what a protein looks like in one stable conformation. This can be misleading, because enzymes in solution are certainly not static.
- Shiven Kapur and Chaitan Khosla are in the Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Email: shiven@stanford.edu
Email: khosla@stanford.edu
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