3j8j: Difference between revisions

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'''Unreleased structure'''
==Tilted state of actin, T1==
<StructureSection load='3j8j' size='340' side='right' caption='[[3j8j]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3j8j]] is a 11 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=3J8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J8J FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j8i|3j8i]], [[3j8k|3j8k]]</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=3j8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j8j RCSB], [http://www.ebi.ac.uk/pdbsum/3j8j PDBsum]</span></td></tr>
</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 ==
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.


The entry 3j8j is ON HOLD
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>


Authors: Galkin, V.E., Orlova, A., Vos, M.R., Schroder, G.F., Egelman, E.H.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Tilted state of actin, T1
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Galkin, V.E]]
__TOC__
[[Category: Egelman, E.H]]
</StructureSection>
[[Category: Schroder, G.F]]
[[Category: Oryctolagus cuniculus]]
[[Category: Egelman, E H]]
[[Category: Galkin, V E]]
[[Category: Orlova, A]]
[[Category: Orlova, A]]
[[Category: Vos, M.R]]
[[Category: Schroder, G F]]
[[Category: Vos, M R]]
[[Category: Actin filament]]
[[Category: Helical polymer]]
[[Category: Structural protein]]
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