+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-30583 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | CryoEM structure of cotton cellulose synthase isoform 7 | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | cellulose synthase / cotton / MEMBRANE PROTEIN | |||||||||
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 | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Guan ZY / Xue Y | |||||||||
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 |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_30583.map.gz | 5.3 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-30583-v30.xml emd-30583.xml | 10.5 KB 10.5 KB | Display Display | EMDB header |
Images | emd_30583.png | 87.4 KB | ||
Filedesc metadata | emd-30583.cif.gz | 5.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30583 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30583 | HTTPS FTP |
-Validation report
Summary document | emd_30583_validation.pdf.gz | 371.2 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_30583_full_validation.pdf.gz | 370.7 KB | Display | |
Data in XML | emd_30583_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | emd_30583_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30583 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30583 | HTTPS FTP |
-Related structure data
Related structure data | 7d5kMC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_30583.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Sample components
-Entire : Cellulose synthase
Entire | Name: Cellulose synthase |
---|---|
Components |
|
-Supramolecule #1: Cellulose synthase
Supramolecule | Name: Cellulose synthase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: Gossypium hirsutum (cotton) |
-Macromolecule #1: Cellulose synthase
Macromolecule | Name: Cellulose synthase / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: cellulose synthase (UDP-forming) |
---|---|
Source (natural) | Organism: Gossypium hirsutum (cotton) |
Molecular weight | Theoretical: 118.129711 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MEASAGLVAG SHNRNELVVI HGHEEPKPLK NLDGQVCEIC GDEIGVTVDG DLFVACNECG FPVCRPCYEY ERREGTQQCP QCKTRYKRL KGSPRVEGDE DEEDVDDIEH EFNIDDEQNK HRNVVESILH GKMSYGRGPE DDETPQIPVI TGVRSRPVSG E FPIAGALA ...String: MEASAGLVAG SHNRNELVVI HGHEEPKPLK NLDGQVCEIC GDEIGVTVDG DLFVACNECG FPVCRPCYEY ERREGTQQCP QCKTRYKRL KGSPRVEGDE DEEDVDDIEH EFNIDDEQNK HRNVVESILH GKMSYGRGPE DDETPQIPVI TGVRSRPVSG E FPIAGALA YGEHMPNASL HKRVHPYPMS ETEGAERWDD KKEGGWKERM DDWKMQQGNL GPEADDAYDD MSMLDEARQP LS RKVPIAS SKINPYRMVI VARLLILAFF LRYRILNPVH DAIGLWLTSV ICEIWFAFSW ILDQFPKWFP IDRETYLDRL SLR YEREGE PNMLAPVDIF VSTVDPMKEP PLVTANTVLS ILAMDYPVDK ISCYISDDGA SMLTFESLSE TAEFARKWVP FCKK FAIEP RAPEMYFTLK VDYLKDKVQP TFVKERRAMK REYEEFKVRI NALVAKAQKV PPEGWIMQDG TPWPGNNTKD HPGMI QVFL GQSGGHDTEG NELPRLVYVS REKRPGFLHH KKAGAMNALV RVSGVLTNAP FMLNLDCDHY INNSKAAREA MCFLMD PQI GRKVCYVQFP QRFDGIDRHD RYANRNTVFF DINMKGLDGI QGPVYVGTGC VFRRQALYGY EPPKGPKRPK MVSCGCC PC FGRRKKDKKY PKNGGNENGP SLEAVEDDKE LLMSQMNFEK KFGQSAIFVT STLMDQGGVP PSSSPAALLK EAIHVISC G YEDKTEWGSE LGWIYGSITE DILTGFKMHC RGWRSIYCMP KLPAFKGSAP INLSDRLNQV LRWALGSVEI FFSRHCPAW YGLKGAKLRW LERFAYVNTT IYPFTSLPLL AYCTLPAICL LTDKFIMPPI STFASLFFIA LFLSIFATGI LELRWSGVSI EEWWRNEQF WVIGGISAHL FAVVQGLLKV LAGIDTNFTV TSKTTDDEEF GELYTFKWTT LLIPPTTVLI INLVGVVAGI S DAINNGYQ SWGPLFGKLF FSFWVIVHLY PFLKGLMGRQ NRTPTIVVIW SVLLASIFSL LWVRIDPFVL KTKGPDTTQC GI NC UniProtKB: Cellulose synthase |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 5 mg/mL |
---|---|
Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |