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-Structure paper
Title | Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana. |
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Journal, issue, pages | PLoS One, Vol. 9, Issue 1, Page e87724, Year 2014 |
Publish date | Jan 27, 2014 |
Authors | Hideki Shigematsu / Kazuko Iida / Masataka Nakano / Pratima Chaudhuri / Hidetoshi Iida / Kuniaki Nagayama / |
PubMed Abstract | Mechanosensing in plants is thought to be governed by sensory complexes containing a Ca²⁺-permeable, mechanosensitive channel. The plasma membrane protein MCA1 and its paralog MCA2 from ...Mechanosensing in plants is thought to be governed by sensory complexes containing a Ca²⁺-permeable, mechanosensitive channel. The plasma membrane protein MCA1 and its paralog MCA2 from Arabidopsis thaliana are involved in mechanical stress-induced Ca²⁺ influx and are thus considered as candidates for such channels or their regulators. Both MCA1 and MCA2 were functionally expressed in Sf9 cells using a baculovirus system in order to elucidate their molecular natures. Because of the abundance of protein in these cells, MCA2 was chosen for purification. Purified MCA2 in a detergent-solubilized state formed a tetramer, which was confirmed by chemical cross-linking. Single-particle analysis of cryo-electron microscope images was performed to depict the overall shape of the purified protein. The three-dimensional structure of MCA2 was reconstructed at a resolution of 26 Å from 5,500 particles and appears to comprise a small transmembrane region and large cytoplasmic region. |
External links | PLoS One / PubMed:24475319 / PubMed Central |
Methods | EM (single particle) |
Resolution | 26.0 Å |
Structure data | EMDB-2313: |
Source |
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