1mdu
From Proteopedia
(New page: 200px<br /> <applet load="1mdu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdu, resolution 2.2Å" /> '''Crystal structure of...) |
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| - | [[Image:1mdu.gif|left|200px]]<br /> | + | [[Image:1mdu.gif|left|200px]]<br /><applet load="1mdu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mdu" size=" | + | |
caption="1mdu, resolution 2.2Å" /> | caption="1mdu, resolution 2.2Å" /> | ||
'''Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)'''<br /> | '''Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Stable oligomers of filamentous actin were obtained by cross-linking | + | Stable oligomers of filamentous actin were obtained by cross-linking F-actin with 1,4-N,N'-phenylenedimaleimide and depolymerization with excess segment-1 of gelsolin. Segment-1-bound and cross-linked actin oligomers containing either two or three actin subunits were purified and shown to nucleate actin assembly. Kinetic assembly data from mixtures of monomeric actin and the actin oligomers fit a nucleation model where cross-linked actin dimer or trimer reacts with an actin monomer to produce a competent nucleus for filament assembly. We report the three-dimensional structure of the segment-1-actin hexamer containing three actin subunits, each with a tightly bound ATP. Comparative analysis of this structure with twelve other actin structures provides an atomic level explanation for the preferential binding of ATP by the segment-1-complexed actin. Although the structure of segment-1-bound actin trimer is topologically similar to the helical model of F-actin (1), it has a distorted symmetry compared with that of the helical model. This distortion results from intercalation of segment-1 between actin protomers that increase the rise per subunit and rotate each of the actin subunits relative to their positions in F-actin. We also show that segment-1 of gelsolin is able to sever actin filaments, although the severing activity of segment-1 is significantly lower than full-length gelsolin. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MDU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, ATP and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MDU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Dawson, J | + | [[Category: Dawson, J F.]] |
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
| - | [[Category: Sablin, E | + | [[Category: Sablin, E P.]] |
| - | [[Category: Spudich, J | + | [[Category: Spudich, J A.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: gelsolin precursor]] | [[Category: gelsolin precursor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:13 2008'' |
Revision as of 11:54, 21 February 2008
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Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)
Contents |
Overview
Stable oligomers of filamentous actin were obtained by cross-linking F-actin with 1,4-N,N'-phenylenedimaleimide and depolymerization with excess segment-1 of gelsolin. Segment-1-bound and cross-linked actin oligomers containing either two or three actin subunits were purified and shown to nucleate actin assembly. Kinetic assembly data from mixtures of monomeric actin and the actin oligomers fit a nucleation model where cross-linked actin dimer or trimer reacts with an actin monomer to produce a competent nucleus for filament assembly. We report the three-dimensional structure of the segment-1-actin hexamer containing three actin subunits, each with a tightly bound ATP. Comparative analysis of this structure with twelve other actin structures provides an atomic level explanation for the preferential binding of ATP by the segment-1-complexed actin. Although the structure of segment-1-bound actin trimer is topologically similar to the helical model of F-actin (1), it has a distorted symmetry compared with that of the helical model. This distortion results from intercalation of segment-1 between actin protomers that increase the rise per subunit and rotate each of the actin subunits relative to their positions in F-actin. We also show that segment-1 of gelsolin is able to sever actin filaments, although the severing activity of segment-1 is significantly lower than full-length gelsolin.
Disease
Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]
About this Structure
1MDU is a Protein complex structure of sequences from Gallus gallus and Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing., Dawson JF, Sablin EP, Spudich JA, Fletterick RJ, J Biol Chem. 2003 Jan 10;278(2):1229-38. Epub 2002 Sep 27. PMID:12356759
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