1omr: Difference between revisions

Revision as of 17:36, 28 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:1omr.png

Template:STRUCTURE 1omr

non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3

Template:ABSTRACT PUBMED 12686556

About this StructureAbout this Structure

1OMR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin., Weiergraber OH, Senin II, Philippov PP, Granzin J, Koch KW, J Biol Chem. 2003 Jun 20;278(25):22972-9. Epub 2003 Apr 9. PMID:12686556

Page seeded by OCA on Mon Jul 28 17:36:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1omr.gif|left|200px]]
+{{Seed}}
+[[Image:1omr.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1omr|  PDB=1omr  |  SCENE=  }}
-'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3'''
+===non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3===
-==Overview==
+<!--
-Recoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_12686556}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12686556 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12686556}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Ef-hand]]
 [[Category: Helix-loop-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:02:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:36:27 2008''