1f7s
From Proteopedia
(New page: 200px<br /><applet load="1f7s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f7s, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1f7s.jpg|left|200px]]<br /><applet load="1f7s" size=" | + | [[Image:1f7s.jpg|left|200px]]<br /><applet load="1f7s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f7s, resolution 2.0Å" /> | caption="1f7s, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF ADF1 FROM ARABIDOPSIS THALIANA'''<br /> | '''CRYSTAL STRUCTURE OF ADF1 FROM ARABIDOPSIS THALIANA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Actin-depolymerizing factor (ADF) and cofilin define a family of | + | Actin-depolymerizing factor (ADF) and cofilin define a family of actin-binding proteins essential for the rapid turnover of filamentous actin in vivo. Here we present the 2.0 A crystal structure of Arabidopsis thaliana ADF1 (AtADF1), the first plant crystal structure from the ADF/cofilin (AC) family. Superposition of the four AC isoform structures permits an accurate sequence alignment that differs from previously reported data for the location of vertebrate-specific inserts and reveals a contiguous, vertebrate-specific surface opposite the putative actin-binding surface. Extending the structure-based sequence alignment to include 30 additional isoforms indicates three major groups: vertebrates, plants, and "other eukaryotes." Within these groups, several structurally conserved residues that are not conserved throughout the entire AC family have been identified. Residues that are highly conserved among all isoforms tend to cluster around the tryptophan at position 90 and a structurally conserved kink in alpha-helix 3. Analysis of surface character shows the presence of a hydrophobic patch and a highly conserved acidic cluster, both of which include several residues previously implicated in actin binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1F7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with LDA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1F7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bowman, G | + | [[Category: Bowman, G D.]] |
| - | [[Category: Chua, N | + | [[Category: Chua, N H.]] |
[[Category: Lindberg, U.]] | [[Category: Lindberg, U.]] | ||
| - | [[Category: Nodelman, I | + | [[Category: Nodelman, I M.]] |
| - | [[Category: Schutt, C | + | [[Category: Schutt, C E.]] |
[[Category: LDA]] | [[Category: LDA]] | ||
[[Category: kink in alpha-helix 3]] | [[Category: kink in alpha-helix 3]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:49 2008'' |
Revision as of 10:35, 21 February 2008
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CRYSTAL STRUCTURE OF ADF1 FROM ARABIDOPSIS THALIANA
Overview
Actin-depolymerizing factor (ADF) and cofilin define a family of actin-binding proteins essential for the rapid turnover of filamentous actin in vivo. Here we present the 2.0 A crystal structure of Arabidopsis thaliana ADF1 (AtADF1), the first plant crystal structure from the ADF/cofilin (AC) family. Superposition of the four AC isoform structures permits an accurate sequence alignment that differs from previously reported data for the location of vertebrate-specific inserts and reveals a contiguous, vertebrate-specific surface opposite the putative actin-binding surface. Extending the structure-based sequence alignment to include 30 additional isoforms indicates three major groups: vertebrates, plants, and "other eukaryotes." Within these groups, several structurally conserved residues that are not conserved throughout the entire AC family have been identified. Residues that are highly conserved among all isoforms tend to cluster around the tryptophan at position 90 and a structurally conserved kink in alpha-helix 3. Analysis of surface character shows the presence of a hydrophobic patch and a highly conserved acidic cluster, both of which include several residues previously implicated in actin binding.
About this Structure
1F7S is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.
Reference
A comparative structural analysis of the ADF/cofilin family., Bowman GD, Nodelman IM, Hong Y, Chua NH, Lindberg U, Schutt CE, Proteins. 2000 Nov 15;41(3):374-84. PMID:11025548
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