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The 0.83 A Resolution Crystal Structure of a-Lytic Protease Reveals the Detailed Structure of the Active
 

Summary: The 0.83 A Resolution Crystal Structure of a-Lytic
Protease Reveals the Detailed Structure of the Active
Site and Identifies a Source of Conformational Strain
This paper is dedicated to Dr Peter A. Kollman, whose dynamic enthusiasm for science and life will
continue to inspire all who knew him.
Cynthia N. Fuhrmann, Brian A. Kelch, Nobuyuki Ota and
David A. Agard*
Howard Hughes Medical
Institute and Department of
Biochemistry and Biophysics
University of California, San
Francisco, 600 16th Street, San
Francisco, CA 94143-2240
USA
The crystal structure of the extracellular bacterial serine protease a-lytic
protease (aLP) has been solved at 0.83 A resolution at pH 8. This ultra-
high resolution structure allows accurate analysis of structural elements
not possible with previous structures. Hydrogen atoms are visible, and
confirm active-site hydrogen-bonding interactions expected for the apo
enzyme. In particular, His57 Nd1

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine