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Crystal Structure of the Catalytic Domain of a Serine Threonine Protein PhosphataseReversible phosphorylation of serine and threonine residues is a well-recognized mechanism in eukaryotic cells for the regulation of cell-cycle progression, cell growth and metabolism. Human serine/threonine phosphatases can be placed into two major families, PPP and PPM. To date the structure on one PPP family member (PPl) has been determined. Here we present the structure of a 323-residue catalytic domain of a second phosphatase belonging to the PPP family of enzyme. catalytic domain of the enzyme has been determined to 1.60Angstrom resolution and refined to R=17.5 and Rfree = 20.8%. The catalytic domain possesses a unique fold consisting of a largely monolithic structure, divisible into closely-associated helical and sheet regions. The catalytic site contains two manganese ions that are involved in substrate binding and catalysis. The enzyme crystallizes as a dimer that completely buries catalytic surfaces of both monomers, Also, the structure shows evidence of some flexibility around the active site cleft that may be related to substrate specificity of this enzyme.
Document ID
20030067738
Acquisition Source
Marshall Space Flight Center
Document Type
Preprint (Draft being sent to journal)
Authors
Swinglel, Mark
(University of South Alabama Mobile, AL, United States)
Honkanel, Richard
(University of South Alabama Mobile, AL, United States)
Ciszak, Ewa
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2003
Subject Category
Inorganic, Organic And Physical Chemistry
Meeting Information
Meeting: American Crystallographic Association (ACA)
Location: Covington, KY
Country: United States
Start Date: July 26, 2003
End Date: July 31, 2003
Sponsors: American Crystallographic Association
Distribution Limits
Public
Copyright
Other

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