1ypr: Difference between revisions
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[[Image:1ypr.gif|left|200px]] | [[Image:1ypr.gif|left|200px]] | ||
'''SACCHAROMYCES CEREVISIAE (YEAST) PROFILIN''' | {{Structure | ||
|PDB= 1ypr |SIZE=350|CAPTION= <scene name='initialview01'>1ypr</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SACCHAROMYCES CEREVISIAE (YEAST) PROFILIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YPR is a [ | 1YPR is a [[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== | ||
Structure determination and characterization of Saccharomyces cerevisiae profilin., Eads JC, Mahoney NM, Vorobiev S, Bresnick AR, Wen KK, Rubenstein PA, Haarer BK, Almo SC, Biochemistry. 1998 Aug 11;37(32):11171-81. PMID:[http:// | Structure determination and characterization of Saccharomyces cerevisiae profilin., Eads JC, Mahoney NM, Vorobiev S, Bresnick AR, Wen KK, Rubenstein PA, Haarer BK, Almo SC, Biochemistry. 1998 Aug 11;37(32):11171-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9698363 9698363] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: profilin]] | [[Category: profilin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:57 2008'' | ||
Revision as of 16:25, 20 March 2008
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SACCHAROMYCES CEREVISIAE (YEAST) PROFILIN
OverviewOverview
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 StructureAbout this Structure
1YPR is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure determination and characterization of Saccharomyces cerevisiae profilin., Eads JC, Mahoney NM, Vorobiev S, Bresnick AR, Wen KK, Rubenstein PA, Haarer BK, Almo SC, Biochemistry. 1998 Aug 11;37(32):11171-81. PMID:9698363
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