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3j8k
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Tilted state of actin, T2== |
| + | <StructureSection load='3j8k' size='340' side='right' caption='[[3j8k]], [[Resolution|resolution]] 12.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3j8k]] 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=3J8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J8K FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j8i|3j8i]], [[3j8j|3j8j]]</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=3j8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j8k RCSB], [http://www.ebi.ac.uk/pdbsum/3j8k 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Egelman, E | + | </StructureSection> |
| - | [[Category: | + | [[Category: Oryctolagus cuniculus]] |
| + | [[Category: Egelman, E H]] | ||
| + | [[Category: Galkin, V E]] | ||
[[Category: Orlova, A]] | [[Category: Orlova, A]] | ||
| - | [[Category: Vos, M | + | [[Category: Schroder, G F]] |
| + | [[Category: Vos, M R]] | ||
| + | [[Category: Actin filament]] | ||
| + | [[Category: Helical polymer]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 13:29, 14 January 2015
Tilted state of actin, T2
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