Protein Engineering, Vol 11, 1129-1135, Copyright © 1998 by Oxford University Press
R Grandori
A robust tool for fold recognition was applied to the systematic analysis
of the sequences below 200 residues encoded by the genome of Mycoplasma
pneumoniae. The goal was to determine the additional information gain
achievable in genome analysis by fold recognition, beyond the intrinsic
limits of homology studies. A list of 124 sequences encoding for soluble
proteins or domains not homologous to each other, or to proteins with known
three-dimensional structure, was analyzed, resulting in significant Z
scores for the energy of the structural models in 12 of these cases. This
result indicates that systematic application of fold recognition techniques
to the analysis of structurally unassigned soluble proteins can lead to
high-confidence structural predictions with an efficiency of about 10%, a
relevant contribution besides the complementary approach of homology
analysis. Four of the predictions presented include mapping of the putative
active site of the target sequence and lead to the detection of probable
catalytic and binding residues. The data are discussed with reference to
the functional implications of the structural models and to the results
reported for the homologous genome of Mycoplasma genitalium.
ARTICLES
Systematic fold recognition analysis of the sequences encoded by the genome of Mycoplasma pneumoniae
Center for Applied Molecular Engineering, Institute for Chemistry and Biochemistry, University of Salzburg, Austria. rita.grandori@jk.uni- linz.ac.at
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