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-Structure paper
Title | Cryo-Electron Tomography of Candida glabrata Plasma Membrane Proteins. |
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Journal, issue, pages | J Fungi (Basel), Vol. 7, Issue 2, Year 2021 |
Publish date | Feb 6, 2021 |
Authors | Cristina Jiménez-Ortigosa / Jennifer Jiang / Muyuan Chen / Xuyuan Kuang / Kelley R Healey / Paul Castellano / Nikpreet Boparai / Steven J Ludtke / David S Perlin / Wei Dai / |
PubMed Abstract | Fungal plasma membrane proteins have long been recognized as targets for the development of antifungal agents. Despite recent progress in experimental approaches and computational structural ...Fungal plasma membrane proteins have long been recognized as targets for the development of antifungal agents. Despite recent progress in experimental approaches and computational structural predictions, our knowledge of the structural dynamics and spatial distribution of these membrane proteins in the context of their native lipid environment remains limited. By applying cryo-electron tomography (cryoET) and subtomogram analysis, we aim to characterize the structural characteristics and spatial distribution of membrane proteins present in plasma membranes. This study has resulted in the identification of the membrane-embedded structure of the fungal H+-ATPase, Pma1. Tomograms of the plasma membrane revealed that Pma1 complexes are heterogeneously distributed as hexamers that cluster into distinct membrane microdomains. This study characterizes fungal membrane proteins in the native cellular landscape and highlights the unique potential of cryoET to advance our understanding of cellular biology and biological systems. |
External links | J Fungi (Basel) / PubMed:33562124 / PubMed Central |
Methods | EM (subtomogram averaging) |
Resolution | 14.0 - 18.0 Å |
Structure data | EMDB-23122: EMDB-23123: |
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