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We just published a paper in which one of the structures had product compound displaced from the active site by a DMSO molecule bound in the oxyanion hole.  The product was bound, but not in the catalytically relevant orientation.

Structural basis for macrolactonization by the pikromycin thioesterase
David L Akey, Jeffrey D Kittendorf, John W Giraldes, Robert A Fecik, David H Sherman, Janet L Smith

Nature Chemical Biology 2, 537 - 542 (01 Oct 2006) Letters



David Akey, Ph.D.
Research Scientist
Janet Smith Laboratory
Life Sciences Institute
University of Michigan
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On Jan 23, 2007, at 12:46 PM, Radisky, Evette S. Ph.D. wrote:

A biochemist friend asked for examples of cases were a protein was
co-crystallized with or soaked in a ligand that bound in the wrong place
- say, because the ligand used wasn't quite the right one or because
other important ligands were absent.
I'm sure such examples are out there, especially when soaks were done at
high concentrations, but I'm having trouble thinking of concrete
examples.
Help?
thanks,
Phoebe Rice


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Phoebe A. Rice
Assoc. Prof., Dept. of Biochemistry & Molecular Biology The University
of Chicago phone 773 834 1723 fax 773 702 0439
http://bmb.bsd.uchicago.edu/index.html
http://www.nasa.gov/mission_pages/cassini/multimedia/pia06064.html