1ypr: Difference between revisions

New page: left|200px<br /><applet load="1ypr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ypr, resolution 2.3Å" /> '''SACCHAROMYCES CEREVIS...
 
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[[Image:1ypr.gif|left|200px]]<br /><applet load="1ypr" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ypr.gif|left|200px]]<br /><applet load="1ypr" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ypr, resolution 2.3&Aring;" />
caption="1ypr, resolution 2.3&Aring;" />
'''SACCHAROMYCES CEREVISIAE (YEAST) PROFILIN'''<br />
'''SACCHAROMYCES CEREVISIAE (YEAST) PROFILIN'''<br />


==Overview==
==Overview==
The structure of profilin from the budding yeast Saccharomyces cerevisiae, has been determined by X-ray crystallography at 2.3 A resolution. The, overall fold of yeast profilin is similar to the fold observed for other, profilin structures. The interactions of yeast and human platelet, profilins with rabbit skeletal muscle actin were characterized by, titration microcalorimetry, fluorescence titrations, and nucleotide, exchange kinetics. The affinity of yeast profilin for rabbit actin (2.9, microM) is approximately 30-fold weaker than the affinity of human, platelet profilin for rabbit actin (0.1 microM), and the relative, contributions of entropic and enthalpic terms to the overall free energy, of binding are different for the two profilins. The titration of, pyrene-labeled rabbit skeletal actin with human profilin yielded a Kd of, 2.8 microM, similar to the Kd of 2.0 microM for the interaction between, yeast profilin and pyrene-labeled yeast actin. The binding data are, discussed in the context of the known crystal structures of profilin and, actin, and the residues present at the actin-profilin interface. The, affinity of yeast profilin for poly-L-proline was determined from, fluorescence measurements and is similar to the reported affinity of, Acanthamoeba profilin for poly-L-proline. Yeast profilin was shown to, catalyze adenine nucleotide exchange from yeast actin almost 2 orders of, magnitude less efficiently than human profilin and rabbit skeletal muscle, actin. The in vivo and in vitro properties of yeast profilin mutants with, altered poly-L-proline and actin binding sites are discussed in the, context of the crystal structure.
The structure of profilin from the budding yeast Saccharomyces cerevisiae has been determined by X-ray crystallography at 2.3 A resolution. The overall fold of yeast profilin is similar to the fold observed for other profilin structures. The interactions of yeast and human platelet profilins with rabbit skeletal muscle actin were characterized by titration microcalorimetry, fluorescence titrations, and nucleotide exchange kinetics. The affinity of yeast profilin for rabbit actin (2.9 microM) is approximately 30-fold weaker than the affinity of human platelet profilin for rabbit actin (0.1 microM), and the relative contributions of entropic and enthalpic terms to the overall free energy of binding are different for the two profilins. The titration of pyrene-labeled rabbit skeletal actin with human profilin yielded a Kd of 2.8 microM, similar to the Kd of 2.0 microM for the interaction between yeast profilin and pyrene-labeled yeast actin. The binding data are discussed in the context of the known crystal structures of profilin and actin, and the residues present at the actin-profilin interface. The affinity of yeast profilin for poly-L-proline was determined from fluorescence measurements and is similar to the reported affinity of Acanthamoeba profilin for poly-L-proline. Yeast profilin was shown to catalyze adenine nucleotide exchange from yeast actin almost 2 orders of magnitude less efficiently than human profilin and rabbit skeletal muscle actin. The in vivo and in vitro properties of yeast profilin mutants with altered poly-L-proline and actin binding sites are discussed in the context of the crystal structure.


==About this Structure==
==About this Structure==
1YPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YPR OCA].  
1YPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPR OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Almo, S.C.]]
[[Category: Almo, S C.]]
[[Category: Eads, J.C.]]
[[Category: Eads, J C.]]
[[Category: Mahoney, N.M.]]
[[Category: Mahoney, N M.]]
[[Category: actin-binding protein]]
[[Category: actin-binding protein]]
[[Category: cytoskeleton]]
[[Category: cytoskeleton]]
[[Category: profilin]]
[[Category: profilin]]


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