6u96: Difference between revisions
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==Actin phalloidin at BeFx state== | ==Actin phalloidin at BeFx state== | ||
<StructureSection load='6u96' size='340' side='right'caption='[[6u96]]' scene=''> | <StructureSection load='6u96' size='340' side='right'caption='[[6u96]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U96 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6U96 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6u96]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U96 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6U96 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u96 OCA], [http://pdbe.org/6u96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u96 RCSB], [http://www.ebi.ac.uk/pdbsum/6u96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u96 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=EEP:'>EEP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u96 OCA], [http://pdbe.org/6u96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u96 RCSB], [http://www.ebi.ac.uk/pdbsum/6u96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u96 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Detailed molecular information on G-actin assembly into filaments (F-actin), and their structure, dynamics, and interactions, is essential for understanding their cellular functions. Previous studies indicate that a flexible DNase I binding loop (D-loop, residues 40-50) plays a major role in actin's conformational dynamics. Phalloidin, a "gold standard" for actin filament staining, stabilizes them and affects the D-loop. Using disulfide crosslinking in yeast actin D-loop mutant Q41C/V45C, light-scattering measurements, and cryoelectron microscopy reconstructions, we probed the constraints of D-loop dynamics and its contribution to F-actin formation/stability. Our data support a model of residues 41-45 distances that facilitate G- to F-actin transition. We report also a 3.3-A resolution structure of phalloidin-bound F-actin in the ADP-Pi-like (ADP-BeFx) state. This shows the phalloidin-binding site on F-actin and how the relative movement between its two protofilaments is restricted by it. Together, our results provide molecular details of F-actin structure and D-loop dynamics. | |||
D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin.,Das S, Ge P, Oztug Durer ZA, Grintsevich EE, Zhou ZH, Reisler E Structure. 2020 May 5;28(5):586-593.e3. doi: 10.1016/j.str.2020.04.004. Epub 2020, Apr 28. PMID:32348747<ref>PMID:32348747</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6u96" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Das S]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Durer | [[Category: Das, S]] | ||
[[Category: Ge P]] | [[Category: Durer, Z A.O]] | ||
[[Category: Grintsevich | [[Category: Ge, P]] | ||
[[Category: Reisler E]] | [[Category: Grintsevich, E E]] | ||
[[Category: Zhou | [[Category: Reisler, E]] | ||
[[Category: Zhou, Z H]] | |||
[[Category: Actin]] | |||
[[Category: Beryllium fluoride]] | |||
[[Category: Phalloidin]] | |||
[[Category: Structural protein]] | |||
