8a2r: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Cryo-EM structure of F-actin in the Mg2+-ADP-BeF3- nucleotide state.== | ==Cryo-EM structure of F-actin in the Mg2+-ADP-BeF3- nucleotide state.== | ||
<StructureSection load='8a2r' size='340' side='right'caption='[[8a2r]]' scene=''> | <StructureSection load='8a2r' size='340' side='right'caption='[[8a2r]], [[Resolution|resolution]] 2.17Å' 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=8A2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A2R FirstGlance]. <br> | <table><tr><td colspan='2'>[[8a2r]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A2R FirstGlance]. <br> | ||
</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=8a2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a2r OCA], [https://pdbe.org/8a2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a2r RCSB], [https://www.ebi.ac.uk/pdbsum/8a2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a2r 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>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8a2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a2r OCA], [https://pdbe.org/8a2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a2r RCSB], [https://www.ebi.ac.uk/pdbsum/8a2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a2r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://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 == | |||
The dynamic turnover of actin filaments (F-actin) controls cellular motility in eukaryotes and is coupled to changes in the F-actin nucleotide state<sup>1-3</sup>. It remains unclear how F-actin hydrolyses ATP and subsequently undergoes subtle conformational rearrangements that ultimately lead to filament depolymerization by actin-binding proteins. Here we present cryo-electron microscopy structures of F-actin in all nucleotide states, polymerized in the presence of Mg<sup>2+</sup> or Ca<sup>2+</sup> at approximately 2.2 A resolution. The structures show that actin polymerization induces the relocation of water molecules in the nucleotide-binding pocket, activating one of them for the nucleophilic attack of ATP. Unexpectedly, the back door for the subsequent release of inorganic phosphate (P<sub>i</sub>) is closed in all structures, indicating that P<sub>i</sub> release occurs transiently. The small changes in the nucleotide-binding pocket after ATP hydrolysis and P<sub>i</sub> release are sensed by a key amino acid, amplified and transmitted to the filament periphery. Furthermore, differences in the positions of water molecules in the nucleotide-binding pocket explain why Ca<sup>2+</sup>-actin shows slower polymerization rates than Mg<sup>2+</sup>-actin. Our work elucidates the solvent-driven rearrangements that govern actin filament assembly and aging and lays the foundation for the rational design of drugs and small molecules for imaging and therapeutic applications. | |||
Structural basis of actin filament assembly and aging.,Oosterheert W, Klink BU, Belyy A, Pospich S, Raunser S Nature. 2022 Nov;611(7935):374-379. doi: 10.1038/s41586-022-05241-8. Epub 2022, Oct 26. PMID:36289337<ref>PMID:36289337</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8a2r" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Belyy A]] | [[Category: Belyy A]] | ||
[[Category: Klink BU]] | [[Category: Klink BU]] | ||