+Open data
-Basic information
Entry | Database: PDB / ID: 7d5k | ||||||
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Title | CryoEM structure of cotton cellulose synthase isoform 7 | ||||||
Components | Cellulose synthase | ||||||
Keywords | MEMBRANE PROTEIN / cellulose synthase / cotton | ||||||
Function / homology | Function and homology information cellulose synthase activity / plant-type primary cell wall biogenesis / cellulose synthase (UDP-forming) / cellulose synthase (UDP-forming) activity / cellulose biosynthetic process / trans-Golgi network / cell wall organization / membrane => GO:0016020 / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Gossypium hirsutum (cotton) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Guan, Z.Y. / Xue, Y. / Yin, P. / Zhang, X.L. | ||||||
Citation | Journal: Plant Biotechnol J / Year: 2021 Title: Structural insights into homotrimeric assembly of cellulose synthase CesA7 from Gossypium hirsutum. Authors: 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 / 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 ...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. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7d5k.cif.gz | 414.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7d5k.ent.gz | 321 KB | Display | PDB format |
PDBx/mmJSON format | 7d5k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7d5k_validation.pdf.gz | 1004.6 KB | Display | wwPDB validaton report |
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Full document | 7d5k_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 7d5k_validation.xml.gz | 59.5 KB | Display | |
Data in CIF | 7d5k_validation.cif.gz | 89.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d5/7d5k ftp://data.pdbj.org/pub/pdb/validation_reports/d5/7d5k | HTTPS FTP |
-Related structure data
Related structure data | 30583MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 118129.711 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gossypium hirsutum (cotton) / Gene: CesA7, LOC107953681 / Cell (production host): HEK293 / Production host: Homo sapiens (human) References: UniProt: L7NUA2, cellulose synthase (UDP-forming) #2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Cellulose synthase / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: Gossypium hirsutum (cotton) |
Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK293 |
Buffer solution | pH: 8 |
Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
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CTF correction | Type: NONE | ||||||||||||||||||||||||
Symmetry | Point symmetry: C3 (3 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 185759 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 66.74 Å2 | ||||||||||||||||||||||||
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