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6bqw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==AlfA Filament bound to AMPPNP== | |
| + | <StructureSection load='6bqw' size='340' side='right' caption='[[6bqw]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6bqw]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></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=6bqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bqw OCA], [http://pdbe.org/6bqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bqw RCSB], [http://www.ebi.ac.uk/pdbsum/6bqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bqw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial actins are an evolutionarily diverse family of ATP-dependent filaments built from protomers with a conserved structural fold. Actin-based segregation systems are encoded on many bacterial plasmids and function to partition plasmids into daughter cells. The bacterial actin AlfA segregates plasmids by a mechanism distinct from other partition systems, dependent on its unique dynamic properties. Here, we report the near-atomic resolution electron cryo-microscopy structure of the AlfA filament, which reveals a strikingly divergent filament architecture resulting from the loss of a subdomain conserved in all other actins and a mode of ATP binding. Its unusual assembly interfaces and nucleotide interactions provide insight into AlfA dynamics, and expand the range of evolutionary variation accessible to actin quaternary structure. | ||
| - | + | Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.,Usluer GD, DiMaio F, Yang SK, Hansen JM, Polka JK, Mullins RD, Kollman JM Proc Natl Acad Sci U S A. 2018 Feb 13. pii: 1715836115. doi:, 10.1073/pnas.1715836115. PMID:29440491<ref>PMID:29440491</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6bqw" style="background-color:#fffaf0;"></div> |
| - | [[Category: Usluer, G | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: DiMaio, F]] | ||
| + | [[Category: Kollman, J M]] | ||
| + | [[Category: Usluer, G D]] | ||
| + | [[Category: Actin]] | ||
| + | [[Category: Cytosolic protein]] | ||
| + | [[Category: Filament]] | ||
| + | [[Category: Plasmid segregation]] | ||
Revision as of 06:34, 28 February 2018
AlfA Filament bound to AMPPNP
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