6BQW
AlfA Filament bound to AMPPNP
Summary for 6BQW
| Entry DOI | 10.2210/pdb6bqw/pdb |
| EMDB information | 7134 |
| Descriptor | Bacterial actin AlfA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total) |
| Functional Keywords | actin, plasmid segregation, filament, cytosolic protein |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 9 |
| Total formula weight | 284909.49 |
| Authors | Usluer, G.D.,Kollman, J.M.,DiMaio, F. (deposition date: 2017-11-28, release date: 2018-02-28, Last modification date: 2024-03-13) |
| Primary citation | Usluer, G.D.,DiMaio, F.,Yang, S.K.,Hansen, J.M.,Polka, J.K.,Mullins, R.D.,Kollman, J.M. Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain. Proc. Natl. Acad. Sci. U.S.A., 115:3356-3361, 2018 Cited by PubMed Abstract: 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. PubMed: 29440491DOI: 10.1073/pnas.1715836115 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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