7D5K
CryoEM structure of cotton cellulose synthase isoform 7
Summary for 7D5K
| Entry DOI | 10.2210/pdb7d5k/pdb |
| EMDB information | 30583 |
| Related PRD ID | PRD_900005 |
| Descriptor | Cellulose synthase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | cellulose synthase, cotton, membrane protein |
| Biological source | Gossypium hirsutum (Upland cotton) |
| Total number of polymer chains | 3 |
| Total formula weight | 356442.91 |
| Authors | Guan, Z.Y.,Xue, Y.,Yin, P.,Zhang, X.L. (deposition date: 2020-09-26, release date: 2021-07-28, Last modification date: 2024-05-29) |
| Primary citation | Zhang, X.,Xue, Y.,Guan, Z.,Zhou, C.,Nie, Y.,Men, S.,Wang, Q.,Shen, C.,Zhang, D.,Jin, S.,Tu, L.,Yin, P.,Zhang, X. Structural insights into homotrimeric assembly of cellulose synthase CesA7 from Gossypium hirsutum. Plant Biotechnol J, 19:1579-1587, 2021 Cited by PubMed Abstract: 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. PubMed: 33638282DOI: 10.1111/pbi.13571 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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