1izr: Difference between revisions

Revision as of 14:17, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1izr.png

Template:STRUCTURE 1izr

F46A mutant of bovine pancreatic ribonuclease AF46A mutant of bovine pancreatic ribonuclease A

Template:ABSTRACT PUBMED 12962489

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 Tue Jul 1 14:17:00 2008

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OCA

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-[[Image:1izr.jpg|left|200px]]
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 {{STRUCTURE_1izr|  PDB=1izr  |  SCENE=  }}
-'''F46A mutant of bovine pancreatic ribonuclease A'''
+===F46A mutant of bovine pancreatic ribonuclease A===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12962489}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12962489 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12962489}}
 ==About this Structure==
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 [[Category: Ribonuclease]]
 [[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 Tue Jul  1 14:17:00 2008''