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TitleAssembly status transition offers an avenue for activity modulation of a supramolecular enzyme.
Journal, issue, pagesElife, Vol. 10, Year 2021
Publish dateDec 13, 2021
AuthorsYao Chen / Weiya Xu / Shuwei Yu / Kang Ni / Guangbiao She / Xiaodong Ye / Qiong Xing / Jian Zhao / Chengdong Huang /
PubMed AbstractNature 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.
External linksElife / PubMed:34898426 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.5 Å
Structure data

31711

7v4h

EMDB-31711, PDB-7v4h:
Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2
Method: EM (single particle) / Resolution: 2.9 Å

31712

7v4i

EMDB-31712, PDB-7v4i:
Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly
Method: EM (single particle) / Resolution: 3.3 Å

31713

7v4j

EMDB-31713, PDB-7v4j:
Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I
Method: EM (single particle) / Resolution: 3.5 Å

31714

7v4k

EMDB-31714, PDB-7v4k:
Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II
Method: EM (single particle)

31715

7v4l

EMDB-31715, PDB-7v4l:
Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • glycine max (soybean)
  • camellia sinensis (black tea)
KeywordsLIGASE / supramolecular enzyme / glutamine synthetase / Glycine max / PLANT PROTEIN / IMMUNE SYSTEM / Camellia sinensis

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