Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
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 p...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2018-03, Vol.115 (13), p.3356-3361 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Usluer, Gülsima D. DiMaio, Frank Yang, Shun Kai Hansen, Jesse M. Polka, Jessica K. Mullins, R. Dyche Kollman, Justin M. |
| description | 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. |
| doi_str_mv | 10.1073/pnas.1715836115 |
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Its unusual assembly interfaces and nucleotide interactions provide insight into AlfA dynamics, and expand the range of evolutionary variation accessible to actin quaternary structure.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1715836115</identifier><identifier>PMID: 29440491</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Actin ; Actins - metabolism ; Actins - ultrastructure ; Adenosine triphosphate ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Assembly ; Bacteria ; Bacterial Proteins - metabolism ; Bacterial Proteins - ultrastructure ; Binding ; Biological Sciences ; Coding ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Cytoskeleton ; Cytoskeleton - metabolism ; Filaments ; Interfaces ; Models, Molecular ; Partitions ; Plasmids ; Protein Domains ; Protein structure ; Quaternary structure ; Sequence Homology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2018-03, Vol.115 (13), p.3356-3361</ispartof><rights>Volumes 1–89 and 106–114, copyright as a collective work only; author(s) retains copyright to individual articles</rights><rights>Copyright National Academy of Sciences Mar 27, 2018</rights><rights>2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c509t-e5ee9eb5596de701a53c977f1df0ecb1de97c8cdef0cd9d50ede9e4babcecda93</citedby><cites>FETCH-LOGICAL-c509t-e5ee9eb5596de701a53c977f1df0ecb1de97c8cdef0cd9d50ede9e4babcecda93</cites><orcidid>0000-0002-7524-8938</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/26508231$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/26508231$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29440491$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Usluer, Gülsima D.</creatorcontrib><creatorcontrib>DiMaio, Frank</creatorcontrib><creatorcontrib>Yang, Shun Kai</creatorcontrib><creatorcontrib>Hansen, Jesse M.</creatorcontrib><creatorcontrib>Polka, Jessica K.</creatorcontrib><creatorcontrib>Mullins, R. Dyche</creatorcontrib><creatorcontrib>Kollman, Justin M.</creatorcontrib><title>Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>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. 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Its unusual assembly interfaces and nucleotide interactions provide insight into AlfA dynamics, and expand the range of evolutionary variation accessible to actin quaternary structure.</description><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Actins - ultrastructure</subject><subject>Adenosine triphosphate</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Assembly</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Binding</subject><subject>Biological Sciences</subject><subject>Coding</subject><subject>Cryoelectron Microscopy</subject><subject>Crystallography, X-Ray</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - metabolism</subject><subject>Filaments</subject><subject>Interfaces</subject><subject>Models, Molecular</subject><subject>Partitions</subject><subject>Plasmids</subject><subject>Protein Domains</subject><subject>Protein structure</subject><subject>Quaternary structure</subject><subject>Sequence Homology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1v1DAQhiMEotvCmRPIEpde0o6dOIkvSKtV-ZCK4FDOlj8mrVeJvdjJSvsb-NM43dICJ1t-n3nHM29RvKFwQaGtLndepQvaUt5VDaX8WbGiIGjZ1AKeFysA1pZdzeqT4jSlLQAI3sHL4oSJuoZa0FXxaxMPobz6StIUZzPNEUnoyXSHRCszYXRqIPniPFkP_ZpE3KMaEpm9-zkjUSnhqIcDUd6S9c33Ujtvnb8lzufapS74dC8ujkon9Oa-gSImKxj3aEmatQ2jcv5V8aLP5vj64Twrfny8utl8Lq-_ffqyWV-XhoOYSuSIAjXnorHYAlW8MqJte2p7QKOpRdGazljswVhhOWB-wVorbdBYJaqz4sPRdzfrEa1BP0U1yF10o4oHGZST_yre3cnbsJe8a0XTsGxw_mAQQ15DmuToksFhUB7DnCTLi2eUM7r0ev8fug1z9Hk8ySjQqmK0gkxdHikTQ0oR-8fPUJBL0HIJWj4FnSve_T3DI_8n2Qy8PQLbNIX4pDccOlbR6jePhLKD</recordid><startdate>20180327</startdate><enddate>20180327</enddate><creator>Usluer, Gülsima D.</creator><creator>DiMaio, Frank</creator><creator>Yang, Shun Kai</creator><creator>Hansen, Jesse M.</creator><creator>Polka, Jessica K.</creator><creator>Mullins, R. 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| subjects | Actin Actins - metabolism Actins - ultrastructure Adenosine triphosphate Adenosine Triphosphate - metabolism Amino Acid Sequence Assembly Bacteria Bacterial Proteins - metabolism Bacterial Proteins - ultrastructure Binding Biological Sciences Coding Cryoelectron Microscopy Crystallography, X-Ray Cytoskeleton Cytoskeleton - metabolism Filaments Interfaces Models, Molecular Partitions Plasmids Protein Domains Protein structure Quaternary structure Sequence Homology |
| title | Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain |
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