Subject: CMNS Distinguished Woman Faculty Lecture

Patricia Babbitt
Department of Bioengineering and Therapeutic Sciences
University of California, San Francisco

Title: How has nature evolved the enzymes required by living systems?
Friday March 25, 2016
12:00 noon
1103 Bioscience Research building

The natural catalytic repertoire includes hundreds of functionally diverse
enzyme superfamilies, each comprised of thousands of sequences and many
different chemical reactions. Studies of some of these superfamilies suggest
that they have evolved using "privileged" scaffolds, structural templates
whose structural folds and active site architectures facilitate catalysis of
common partial reactions or other chemical capabilities. Evolutionary
divergence of the ancestral forms of these scaffolds are then thought to have
lead to the variations in topology, active site architecture, and specificity
determinants that are seen in contemporary superfamily members that catalyze
quite different chemical reactions. Using protein similarity networks, we
have computationally investigated on a global scale structure-function
relationships in several of these superfamilies. Mapping many types of
functional information to these networks enables a large-scale view of
functional trends from the context of sequence and structure similarity.
Interactive exploration of the networks provide clues for prediction of
function for proteins of unknown function as well as offering a new and
powerful context for probing how nature has remodeled these structures to
enable new chemistry. We describe what we have learned from investigation of
a varied set of these superfamilies and provide examples for how the results
can be applied to guide the choice of informative targets for biochemical and
structural characterization and, using evolutionary lessons from nature, to
inform protein engineering in the lab.

Contact Person: Gene Ferrick
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