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1acf
From Proteopedia
(New page: 200px<br /><applet load="1acf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1acf, resolution 2.0Å" /> '''ACANTHAMOEBA CASTELLA...) |
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| - | [[Image:1acf.gif|left|200px]]<br /><applet load="1acf" size=" | + | [[Image:1acf.gif|left|200px]]<br /><applet load="1acf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1acf, resolution 2.0Å" /> | caption="1acf, resolution 2.0Å" /> | ||
'''ACANTHAMOEBA CASTELLANII PROFILIN IB'''<br /> | '''ACANTHAMOEBA CASTELLANII PROFILIN IB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We determined the structures of Acanthamoeba profilin I and profilin II by | + | We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin. |
==About this Structure== | ==About this Structure== | ||
| - | 1ACF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http:// | + | 1ACF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACF OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Acanthamoeba castellanii]] | [[Category: Acanthamoeba castellanii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
| - | [[Category: Fedorov, A | + | [[Category: Fedorov, A A.]] |
| - | [[Category: Graupe, M | + | [[Category: Graupe, M H.]] |
| - | [[Category: Lattman, E | + | [[Category: Lattman, E E.]] |
| - | [[Category: Magnus, K | + | [[Category: Magnus, K A.]] |
| - | [[Category: Pollard, T | + | [[Category: Pollard, T D.]] |
[[Category: actin-binding protein]] | [[Category: actin-binding protein]] | ||
[[Category: profilin]] | [[Category: profilin]] | ||
[[Category: protein binding]] | [[Category: protein binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:07 2008'' |
Revision as of 09:43, 21 February 2008
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ACANTHAMOEBA CASTELLANII PROFILIN IB
Overview
We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.
About this Structure
1ACF is a Single protein structure of sequence from Acanthamoeba castellanii. Full crystallographic information is available from OCA.
Reference
X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates., Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:8078936
Page seeded by OCA on Thu Feb 21 11:43:07 2008
