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-Structure paper
タイトル | Structural insights into homotrimeric assembly of cellulose synthase CesA7 from Gossypium hirsutum. |
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ジャーナル・号・ページ | Plant Biotechnol J, Vol. 19, Issue 8, Page 1579-1587, Year 2021 |
掲載日 | 2021年4月5日 |
![]() | Xiangnan Zhang / Yuan Xue / Zeyuan Guan / Chen Zhou / Yangfan Nie / She Men / Qiang Wang / Cuicui Shen / Delin Zhang / Shuangxia Jin / Lili Tu / Ping Yin / Xianlong Zhang / ![]() |
PubMed 要旨 | Cellulose is one of the most abundant organic polymers in nature. It contains multiple β-1,4-glucan chains synthesized by cellulose synthases (CesAs) on the plasma membrane of higher plants. CesA ...Cellulose is one of the most abundant organic polymers in nature. It contains multiple β-1,4-glucan chains synthesized by cellulose synthases (CesAs) on the plasma membrane of higher plants. CesA subunits assemble into a pseudo-sixfold symmetric cellulose synthase complex (CSC), known as a 'rosette complex'. The structure of CesA remains enigmatic. Here, we report the cryo-EM structure of the homotrimeric CesA7 from Gossypium hirsutum at 3.5-angstrom resolution. The GhCesA7 homotrimer shows a C3 symmetrical assembly. Each protomer contains seven transmembrane helices (TMs) which form a channel potentially facilitating the release of newly synthesized glucans. The cytoplasmic glycosyltransferase domain (GT domain) of GhCesA7 protrudes from the membrane, and its catalytic pocket is directed towards the TM pore. The homotrimer GhCesA7 is stabilized by the transmembrane helix 7 (TM7) and the plant-conserved region (PCR) domains. It represents the building block of CSCs and facilitates microfibril formation. This structure provides insight into how eukaryotic cellulose synthase assembles and provides a mechanistic basis for the improvement of cotton fibre quality in the future. |
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手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | EMDB-30583, PDB-7d5k: |
由来 |
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![]() | MEMBRANE PROTEIN / cellulose synthase / cotton |