title: Crystal structure of a two-subunit TrkA octameric gating ring assembly.
abstract: The TM1088 locus of T. maritima codes for two proteins designated TM1088A and TM1088B, which combine to form the cytosolic portion of a putative Trk K+ transporter. We report the crystal structure of this assembly to a resolution of 3.45 Å. The high resolution crystal structures of the components of the assembly, TM1088A and TM1088B, were also determined independently to 1.50 Å and 1.55 Å, respectively. The TM1088 proteins are structurally homologous to each other and to other K+ transporter proteins, such as TrkA. These proteins form a cytosolic gating ring assembly that controls the flow of K+ ions across the membrane. TM1088 represents the first structure of a two-subunit Trk assembly. Despite the atypical genetics and chain organization of the TM1088 assembly, it shares significant structural homology and an overall quaternary organization with other single-subunit K+ gating ring assemblies. This structure provides the first structural insights into what may be an evolutionary ancestor of more modern single-subunit K+ gating ring assemblies.
authors.affiliation: The Joint Center for Structural Genomics, and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
authors.forename: Marc C
authors.initials: MC
authors.lastname: Deller
authors.affiliation: The Joint Center for Structural Genomics, and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
authors.forename: Hope A
authors.initials: HA
authors.lastname: Johnson
authors.affiliation: The Joint Center for Structural Genomics, and Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, United States of America.
authors.forename: Mitchell D
authors.initials: MD
authors.lastname: Miller
authors.affiliation: Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California, United States of America.
authors.forename: Glen
authors.initials: G
authors.lastname: Spraggon
authors.affiliation: The Joint Center for Structural Genomics, and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
authors.forename: Marc-André
authors.initials: MA
authors.lastname: Elsliger
authors.affiliation: The Joint Center for Structural Genomics, and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
authors.forename: Ian A
authors.initials: IA
authors.lastname: Wilson
authors.affiliation: The Joint Center for Structural Genomics, and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America; Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California, United States of America.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Lesley
mesh_terms: D002846:Chromatography, Affinity; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D020917:Receptor, trkA / Q000737:chemistry*
chemical_list: D020917:Receptor, trkA
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