{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Akkaladevi N"],"funding":["HHS | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e00593-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5809691"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["200(5)"],"pubmed_abstract":["Transmembrane bacterial chemoreceptors are extended, rod-shaped homodimers with ligand-binding sites at one end and interaction sites for signaling complex formation and histidine kinase control at the other. There are atomic-resolution structures of chemoreceptor fragments but not of intact, membrane-inserted receptors. Electron tomography of <i>in vivo</i> signaling complex arrays lack distinct densities for chemoreceptor rods away from the well-ordered base plate region, implying structural heterogeneity. We used negative staining, transmission electron microscopy, and image analysis to characterize the molecular shapes of intact homodimers of the <i>Escherichia coli</i> aspartate receptor Tar rendered functional by insertion into nanodisc-provided <i>E. coli</i> lipid bilayers. Single-"],"journal":["Journal of bacteriology"],"pubmed_title":["Flexible Hinges in Bacterial Chemoreceptors."],"pmcid":["PMC5809691"],"funding_grant_id":["GM29963","R37 GM029963","R01 GM029963"],"pubmed_authors":["Hazelbauer GL","White TA","Stalla D","Bunyak F","Akkaladevi N"],"additional_accession":[]},"is_claimable":false,"name":"Flexible Hinges in Bacterial Chemoreceptors.","description":"Transmembrane bacterial chemoreceptors are extended, rod-shaped homodimers with ligand-binding sites at one end and interaction sites for signaling complex formation and histidine kinase control at the other. There are atomic-resolution structures of chemoreceptor fragments but not of intact, membrane-inserted receptors. Electron tomography of <i>in vivo</i> signaling complex arrays lack distinct densities for chemoreceptor rods away from the well-ordered base plate region, implying structural heterogeneity. We used negative staining, transmission electron microscopy, and image analysis to characterize the molecular shapes of intact homodimers of the <i>Escherichia coli</i> aspartate receptor Tar rendered functional by insertion into nanodisc-provided <i>E. coli</i> lipid bilayers. Single-","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Mar","modification":"2026-05-06T03:45:21.471Z","creation":"2019-03-26T23:49:44Z"},"accession":"S-EPMC5809691","cross_references":{"pubmed":["29229700"],"doi":["10.1128/JB.00593-17","10.1128/jb.00593-17"]}}