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-Structure paper
タイトル | The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat. |
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ジャーナル・号・ページ | Nat Commun, Vol. 4, Page 1766, Year 2013 |
掲載日 | 2013年11月26日 |
著者 | Hiroshi Suzuki / Yasuyuki Ito / Yuji Yamazaki / Katsuhiko Mineta / Masami Uji / Kazuhiro Abe / Kazutoshi Tani / Yoshinori Fujiyoshi / Sachiko Tsukita / |
PubMed 要旨 | Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena ...Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer. |
リンク | Nat Commun / PubMed:23612307 / PubMed Central |
手法 | EM (電子線結晶学) |
解像度 | 7.0 - 10.0 Å |
構造データ | EMDB-2314: EMDB-2315: |
由来 |
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