NDLI: Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism.

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Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism.

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Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Strynadka, N. C. Paetzel, M.
Description	Country affiliation: Canada Author Affiliation: Paetzel M ( Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.)
Abstract	Escherichia coli signal peptidase (SPase) and E. coli UmuD protease are members of an evolutionary clan of serine proteases that apparently utilize a serine-lysine catalytic dyad mechanism. Recently, the crystallographic structure of a SPase inhibitor complex was solved elucidating the catalytic residues and the substrate binding subsites. Here we show a detailed comparison of the E. coli SPase structure to the native E. coli UmuD' structure. The comparison reveals that despite a very low sequence identity these functionally diverse enzymes share the same protein fold within their catalytic core and allows by analogy for the assignment of the cleavage-site orientation and substrate binding subsites in the UmuD(D') protease. The structural alignment of SPase and UmuD' predicts important mechanistic and structural similarities and differences within these newly characterized families of serine proteases.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	8
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1999-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Lysine Membrane Proteins Serine Endopeptidases Chemistry Serine Amino Acid Sequence Binding Sites Escherichia Coli Enzymology Escherichia Coli Proteins Models, Molecular Molecular Sequence Data Protein Structure, Secondary Sequence Alignment Sequence Homology, Amino Acid Metabolism Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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