1cu2
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T4 LYSOZYME MUTANT L84M
OverviewOverview
In an attempt to identify a systematic relation between the structure of a, protein and its folding kinetics, the rate of folding was determined for, 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type, residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine., Methionine, which approximated the size of the original side chain but, which is of different shape and flexibility, was also substituted at most, of the same sites. Mutations that substantially destabilize the protein, and are located in the carboxy-terminal domain generally slow the rate of, folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little, effect on stability tend to have little effect on the rate, no matter, where they are located. These results suggest that, at the rate-limiting, step, elements of structure in the C-terminal domain are formed and have a, structure similar to that of the fully folded protein. Consistent with, this, two variants that somewhat increase the rate of folding (Phe104 -->, Met and Val149 --> Met) are located within the carboxy-terminal domain and, maintain or improve packing with very little perturbation of the wild-type, structure.
About this StructureAbout this Structure
1CU2 is a Single protein structure of sequence from Bacteriophage t4 with CL and HED as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding., Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW, Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:10545167
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