This title appears in the Scientific Report :
2003
Please use the identifier:
http://hdl.handle.net/2128/2643 in citations.
Please use the identifier: http://dx.doi.org/10.1074/jbc.M300447200 in citations.
Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin
Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin
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...
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Personal Name(s): | Weiergräber, O. H. |
---|---|
Senin, I. I. / Philippov, P. P. / Granzin, J. / Koch, K.-W. | |
Contributing Institute: |
Zelluläre Signalverarbeitung; IBI-1 Biologische Strukturforschung; IBI-2 |
Published in: | The @journal of biological chemistry, 278 (2003) S. 22972 - 22979 |
Imprint: |
Bethesda, Md.
Soc.
2003
|
Physical Description: |
22972 - 22979 |
DOI: |
10.1074/jbc.M300447200 |
PubMed ID: |
12686556 |
Document Type: |
Journal Article |
Research Program: |
Neurowissenschaften |
Series Title: |
Journal of Biological Chemistry
278 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1074/jbc.M300447200 in citations.
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. |