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- EMDB-31711: Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 -
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Open data
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Basic information
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Title | Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 | |||||||||
![]() | GmGS Beta2 | |||||||||
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![]() | supramolecular enzyme / glutamine synthetase / Glycine max / PLANT PROTEIN / LIGASE | |||||||||
Function / homology | ![]() glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / ATP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Xu W / Chen Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme. Authors: Yao Chen / Weiya Xu / Shuwei Yu / Kang Ni / Guangbiao She / Xiaodong Ye / Qiong Xing / Jian Zhao / Chengdong Huang / ![]() Abstract: Nature has evolved many supramolecular proteins assembled in certain, sometimes even seemingly oversophisticated, morphological manners. The rationale behind such evolutionary efforts is often poorly ...Nature has evolved many supramolecular proteins assembled in certain, sometimes even seemingly oversophisticated, morphological manners. The rationale behind such evolutionary efforts is often poorly understood. Here, we provide atomic-resolution insights into how the dynamic building of a structurally complex enzyme with higher order symmetry offers amenability to intricate regulation. We have established the functional coupling between enzymatic activity and protein morphological states of glutamine synthetase (GS), an old multi-subunit enzyme essential for cellular nitrogen metabolism. Cryo-EM structure determination of GS in both the catalytically active and inactive assembly states allows us to reveal an unanticipated self-assembly-induced disorder-order transition paradigm, in which the remote interactions between two subcomplex entities significantly rigidify the otherwise structurally fluctuating active sites, thereby regulating activity. We further show in vivo evidences that how the enzyme morphology transitions could be modulated by cellular factors on demand. Collectively, our data present an example of how assembly status transition offers an avenue for activity modulation, and sharpens our mechanistic understanding of the complex functional and regulatory properties of supramolecular enzymes. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 482.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9 KB 9 KB | Display Display | ![]() |
Images | ![]() | 239.7 KB | ||
Filedesc metadata | ![]() | 4.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 562.5 KB | Display | ![]() |
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Full document | ![]() | 562 KB | Display | |
Data in XML | ![]() | 8 KB | Display | |
Data in CIF | ![]() | 9.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7v4hMC ![]() 7v4iC ![]() 7v4jC ![]() 7v4kC ![]() 7v4lC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | GmGS Beta2 | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.505 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : GmGS Beta2
Entire | Name: GmGS Beta2 |
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Components |
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-Supramolecule #1: GmGS Beta2
Supramolecule | Name: GmGS Beta2 / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Glutamine synthetase
Macromolecule | Name: Glutamine synthetase / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO / EC number: glutamine synthetase |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 39.184859 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSLLSDLINL NLSDTTEKVI AEYIWIGGSG MDLRSKARTL PGPVSDPSKL PKWNYDGSST GQAPGEDSEV IIYPQAIFRD PFRRGNNIL VICDTYTPAG EPIPTNKRHD AAKVFSHPDV VAEETWYGIE QEYTLLQKDI QWPLGWPVGG FPGPQGPYYC G VGADKAFG ...String: MSLLSDLINL NLSDTTEKVI AEYIWIGGSG MDLRSKARTL PGPVSDPSKL PKWNYDGSST GQAPGEDSEV IIYPQAIFRD PFRRGNNIL VICDTYTPAG EPIPTNKRHD AAKVFSHPDV VAEETWYGIE QEYTLLQKDI QWPLGWPVGG FPGPQGPYYC G VGADKAFG RDIVDAHYKA CLYAGINISG INGEVMPGQW EFQVGPSVGI SAGDEVWAAR YILERITEIA GVVVSFDPKP IQ GDWNGAG AHTNYSTKSM RNDGGYEVIK TAIEKLGKRH KEHIAAYGEG NERRLTGRHE TADINTFLWG VANRGASVRV GRD TEKAGK GYFEDRRPAS NMDPYVVTSM IADTTILWKP UniProtKB: Glutamine synthetase |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 51.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 104717 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |