1f7s: Difference between revisions

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==CRYSTAL STRUCTURE OF ADF1 FROM ARABIDOPSIS THALIANA==
==CRYSTAL STRUCTURE OF ADF1 FROM ARABIDOPSIS THALIANA==
<StructureSection load='1f7s' size='340' side='right' caption='[[1f7s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1f7s' size='340' side='right'caption='[[1f7s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f7s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7S FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cof|1cof]], [[1ahq|1ahq]], [[1cnu|1cnu]], [[1ak6|1ak6]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7s OCA], [http://pdbe.org/1f7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f7s RCSB], [http://www.ebi.ac.uk/pdbsum/1f7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7s ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7s OCA], [https://pdbe.org/1f7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7s RCSB], [https://www.ebi.ac.uk/pdbsum/1f7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ADF1_ARATH ADF1_ARATH]] Actin-depolymerizing protein. Stimulates F-actin depolymerization. Involved in plant development, cell organ expansion and flowering by controlling breakdown of thick actin cables.<ref>PMID:11402164</ref>
[https://www.uniprot.org/uniprot/ADF1_ARATH ADF1_ARATH] Actin-depolymerizing protein. Stimulates F-actin depolymerization. Involved in plant development, cell organ expansion and flowering by controlling breakdown of thick actin cables.<ref>PMID:11402164</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f7s_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f7s_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7s ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7s ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11025548</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f7s" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bowman, G D]]
[[Category: Arabidopsis thaliana]]
[[Category: Chua, N H]]
[[Category: Large Structures]]
[[Category: Lindberg, U]]
[[Category: Bowman GD]]
[[Category: Nodelman, I M]]
[[Category: Chua NH]]
[[Category: Schutt, C E]]
[[Category: Lindberg U]]
[[Category: Kink in alpha-helix 3]]
[[Category: Nodelman IM]]
[[Category: Plant protein]]
[[Category: Schutt CE]]

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