Crystal structure of a two-subunit TrkA octameric gating ring assembly

Deller, Marc C.; Johnson, Hope A.; Miller, Mitchell D.; Spraggon, Glen; Elsliger, Marc -André; Wilson, Ian A.; Lesley, Scott A.; Ye, Sheng

doi:10.1371/journal.pone.0122512

Title: Crystal structure of a two-subunit TrkA octameric gating ring assembly

Journal Article · Tue Mar 31 00:00:00 EDT 2015 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0122512· OSTI ID:1211628

Deller, Marc C. ^[1]; Johnson, Hope A. ^[2]; Miller, Mitchell D. ^[3]; Spraggon, Glen ^[4]; Elsliger, Marc -André ^[1]; Wilson, Ian A. ^[1]; Lesley, Scott A. ^[5]; Ye, Sheng ^[6]

Scripps Research Inst., La Jolla, CA (United States). The Joint Center for Structural Genomics, and Dept. of Integrative Structural and Computional Biology.
Scripps Research Inst., La Jolla, CA (United States). The Joint Center for Structural Genomics, and Dept. of Integrative Structural and Computional Biology; California State Univ., Fullerton, CA (United States)
SLAC National Accelerator Lab., Menlo Park, CA (United States). The Joint Center for Structural Genomics, and Stanford Synchrotron Radiation Lightsource; Rice Univ., Houston, TX (United States)
Genomics Inst. of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
Scripps Research Inst., La Jolla, CA (United States). The Joint Center for Structural Genomics, and Dept. of Integrative Structural and Computional Biology; Genomics Inst. of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
Zhejiang Univ., Hangzhou (China)

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.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States); Protein Structure Initiative of the National Institute of General Medical Sciences, National institutes of Health (NIH)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC03-76SF00098; U54 GM094586

OSTI ID:: 1211628

Journal Information:: PLoS ONE, Vol. 10, Issue 3; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 1 work

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