1izp
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F46L mutant of bovine pancreatic ribonuclease A
OverviewOverview
The Phe46 residue, located in the hydrophobic core of RNase A, was, replaced with other hydrophobic residues, leucine, valine, or alanine, and, their X-ray crystallographic structures were determined up to 1.50-1.80 A, resolution in an attempt to examine the relationship between structural, changes and conformational stability or folding kinetics. The backbone, structure of F46L, F46V, and F46A was indistinguishable from that of the, wild-type enzyme, retaining the correct active site structure. However, one water molecule was included in the hydrophobic core of F46A, forming, two hydrogen bonds with the backbone peptide chain. The side chain of, Met29 in F46V and F46A adopted two different conformations in an equal, occupancy. A trapped water molecule and two conformations of Met29, represent changes that minimize the cavity volume. Nevertheless, the, replacement of Phe46 with the above residues resulted in a marked decrease, in both thermal stability and folding reaction. Thus, Phe46 ensures the, thermal stability and the rapid and correct folding of RNase A by the role, it plays in forming a highly packed, hydrophobic core.
About this StructureAbout this Structure
1IZP is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
ReferenceReference
Minimization of cavity size ensures protein stability and folding: structures of Phe46-replaced bovine pancreatic RNase A., Kadonosono T, Chatani E, Hayashi R, Moriyama H, Ueki T, Biochemistry. 2003 Sep 16;42(36):10651-8. PMID:12962489
Page seeded by OCA on Tue Nov 20 17:48:33 2007