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        <datestamp>2026-09-15T19:57:49Z</datestamp>
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          <dc:title>Data for Alternative architecture of the E. coli chemosensory array</dc:title>
          <dc:creator>Keith Cassidy (24939796)</dc:creator>
          <dc:creator>Alister Burt (6242912)</dc:creator>
          <dc:creator>Phillip J. Stansfeld (1267617)</dc:creator>
          <dc:creator>Irina Gutsche (207422)</dc:creator>
          <dc:subject>Escherichia coli</dc:subject>
          <dc:subject>Chemical ecology</dc:subject>
          <dc:subject>Chemotaxis</dc:subject>
          <dc:subject>Cryoelectronics</dc:subject>
          <dc:subject>Tomography</dc:subject>
          <dc:subject>Molecules -- Models</dc:subject>
          <dc:subject>Migrated from ePrints</dc:subject>
          <dc:description>Chemotactic responses in motile bacteria are the result of sophisticated signal transduction by large, highly organized arrays of sensory proteins. Despite tremendous progress in the understanding of chemosensory array structure and function, a structural basis for the heightened sensitivity of networked chemoreceptors is not yet complete. Here we present cryo-electron tomography visualisations of native-state chemosensory arrays in E. coli minicells. Strikingly, these arrays exhibit a p2-symmetric array architecture that differs markedly from the p6-symmetric architecture previously described in E. coli . Based on this data, we propose molecular models of this alternative architecture and the canonical p6-symmetric assembly. We evaluate our observations and each model in the context of previously published data, assessing the functional implications of an alternative architecture and effects for future studies.&lt;br&gt;&lt;br&gt;Data record consists of data in pdb format. We present molecular models for extended patches of the E. coli chemosensory array. The models display either the canonical p6-symmetric architecture or an alternative p2-symmetric architecture recently observed in E. coli minicells. For more information, please see the associated BioRxiv preprint. Residue coverage: Tsr chemoreceptor (residues 340-440); CheA kinase (residues 264-646), CheW adaptor protein (residues 14-158). PDB naming convention: Tsr chemoreceptors (chain T), CheA kinases (chain A), CheW adaptor proteins (chain W). Individual molecules may be obtained using the 'segname' field in each pdb.</dc:description>
          <dc:date>2026-09-15T19:57:49Z</dc:date>
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          <dc:rights>CC BY 4.0</dc:rights>
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