1izr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1izr.jpg|left|200px]] | [[Image:1izr.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1izr", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1izr| PDB=1izr | SCENE= }} | ||
}} | |||
'''F46A mutant of bovine pancreatic ribonuclease A''' | '''F46A mutant of bovine pancreatic ribonuclease A''' | ||
| Line 31: | Line 28: | ||
[[Category: Moriyama, H.]] | [[Category: Moriyama, H.]] | ||
[[Category: Ueki, T.]] | [[Category: Ueki, T.]] | ||
[[Category: | [[Category: Bovine pancrea]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Ribonuclease]] | ||
[[Category: | [[Category: Rnase some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:37:55 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:37, 2 May 2008
F46A 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
1IZR is a Single protein structure of sequence from Bos taurus. 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 Fri May 2 20:37:55 2008