2acg
From Proteopedia
(New page: 200px<br /><applet load="2acg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2acg, resolution 2.5Å" /> '''ACANTHAMOEBA CASTELLA...) |
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| - | [[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size=" | + | [[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2acg, resolution 2.5Å" /> | caption="2acg, resolution 2.5Å" /> | ||
'''ACANTHAMOEBA CASTELLANII PROFILIN II'''<br /> | '''ACANTHAMOEBA CASTELLANII PROFILIN II'''<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== | ||
| - | 2ACG 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:// | + | 2ACG 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=2ACG OCA]. |
==Reference== | ==Reference== | ||
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[[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 16:25:59 2008'' |
Revision as of 14:26, 21 February 2008
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ACANTHAMOEBA CASTELLANII PROFILIN II
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
2ACG 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
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