3j8i

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<SX load='3j8i' size='340' side='right' viewer='molstar' caption='[[3j8i]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
<SX load='3j8i' size='340' side='right' viewer='molstar' caption='[[3j8i]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j8i]] is a 5 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=3J8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J8I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j8i]] 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=3J8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J8I FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j8j|3j8j]], [[3j8k|3j8k]]</td></tr>
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<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=3j8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8i OCA], [http://pdbe.org/3j8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j8i RCSB], [http://www.ebi.ac.uk/pdbsum/3j8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j8i ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8i OCA], [https://pdbe.org/3j8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j8i RCSB], [https://www.ebi.ac.uk/pdbsum/3j8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j8i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural heterogeneity. We have used a direct electron detector, cryo-electron microscopy, and the forces imposed on actin filaments in thin films to reconstruct one state of the filament at 4.7 A resolution, which allows for building a reliable pseudo-atomic model of F-actin. We also report a different state of the filament where actin protomers adopt a conformation observed in the crystal structure of the G-actin-profilin complex with an open ATP-binding cleft. Comparison of the two structural states provides insights into ATP-hydrolysis and filament dynamics. The atomic model provides a framework for understanding why every buried residue in actin has been under intense selective pressure.
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Near-atomic resolution for one state of f-actin.,Galkin VE, Orlova A, Vos MR, Schroder GF, Egelman EH Structure. 2015 Jan 6;23(1):173-82. doi: 10.1016/j.str.2014.11.006. Epub 2014 Dec, 18. PMID:25533486<ref>PMID:25533486</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3j8i" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Actin 3D structures|Actin 3D structures]]
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== References ==
 
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<references/>
 
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__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Galkin, V E]]
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[[Category: Galkin VE]]
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[[Category: F-actin]]
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[[Category: Helical polymer]]
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[[Category: Structural protein]]
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Current revision

Near-Atomic Resolution for One State of F-Actin

3j8i, resolution 4.70Å

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OCA

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