146l
ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME
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OverviewOverview
To understand better how the packing of side chains within the core, influences protein structure and stability, the crystal structures were, determined for eight variants of T4 lysozyme, each of which contains three, to five substitutions at adjacent interior sites. Concerted main-chain and, side-chain displacements, with movements of helical segments as large as, 0.8 angstrom, were observed. In contrast, the angular conformations of the, mutated side chains tended to remain unchanged, with torsion angles within, 20 degrees of those in the wild-type structure. These observations suggest, that not only the rotation of side chains but also movements of the main, chain must be considered in the evaluation of which amino acid sequences, are compatible with a given protein fold.
About this StructureAbout this Structure
146L is a Single protein structure of sequence from Enterobacteria phage t2 with CL and BME as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme., Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW, Science. 1993 Dec 10;262(5140):1715-8. PMID:8259514
Page seeded by OCA on Tue Nov 20 10:27:30 2007