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J. Biol. Chem., Vol. 275, Issue 22, 16408-16413, June 2, 2000
From the PI-SceI is a member of a class of proteins
(inteins) that excise themselves from a precursor protein and in the
process ligate the flanking protein sequences (exteins). We report here
the 2.1-Å resolution crystal structure of a PI-SceI miniprecursor
(VMA29) containing 10 N-terminal extein residues and 4 C-terminal
extein residues. Mutations at the N- and C-terminal splicing junctions, blocking in vivo protein splicing, allowed the
miniprecursor to be purified and crystallized. The structure reveals
both the N- and C-terminal scissile peptide bonds to be in distorted
trans conformations ( The atomic coordinates and structure factors (code 1EF0) have
been deposited in the Protein Data Bank, Research Collaboratory for
Structural Bioinformatics, Rutgers University, New Brunswick, NJ
(http://www.rcsb.org).
Structural Insights into the Protein Splicing Mechanism of
PI-SceI*
,¶
Howard Hughes Medical Institute and
Department of Biochemistry, Baylor College of Medicine,
Houston, Texas 77030 and § New England Biolabs, Inc.,
Beverly, Massachusetts 01915
100°). Modeling of the
wild-type PI-SceI based on the VMA29 structure indicates a large
conformational change (movement of >9 Å) must occur to allow
transesterification to be completed. A zinc atom was discovered at the
C-terminal splicing junction. Residues Cys455,
His453, and Glu80 along with a water molecule
(Wat53) chelate the zinc atom. The crystal structure of
VMA29 has captured the intein in its pre-spliced state.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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