View source for 5oof


==Cryo-EM structure of F-actin in complex with ADP-BeFx==
<SX load='5oof' size='340' side='right' viewer='molstar' caption='[[5oof]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oof]] 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=5OOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OOF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=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=5oof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oof OCA], [https://pdbe.org/5oof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oof RCSB], [https://www.ebi.ac.uk/pdbsum/5oof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oof ProSAT]</span></td></tr>
</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.
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== Publication Abstract from PubMed ==
The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (Pi) release results in a gradient of ATP, ADP-Pi and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the gamma-phosphate. Nucleotide hydrolysis and Pi release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction.

Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.,Merino F, Pospich S, Funk J, Wagner T, Kullmer F, Arndt HD, Bieling P, Raunser S Nat Struct Mol Biol. 2018 Jun;25(6):528-537. doi: 10.1038/s41594-018-0074-0. Epub, 2018 Jun 4. PMID:29867215<ref>PMID:29867215</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Actin 3D structures|Actin 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Arndt H-D]]
[[Category: Bieling P]]
[[Category: Funk J]]
[[Category: Kuellmer F]]
[[Category: Merino F]]
[[Category: Pospich S]]
[[Category: Raunser S]]