Journal: eLife
Article Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme
doi: 10.7554/eLife.72535
Figure Lengend Snippet: ( a ) Structure alignment of three CsGSIb Pen structures determined using Cryo-EM. Left: Topview; Right: Sideview. These three structures, colored in golden, pink and purple, respectively, are highly similar to each other, with only a few structural variations at the peripheral regions. ( b–d ) Structure comparison of three structures of CsGSIb pentamer in isolation (colored the same as in a ) with that in the context of decamer (in color of green). Upper: Topview; Lower: Sideview. Note a large portion is missing in the structure of CsGSIb Pen arising from electron density missing, indicating those regions are highly dynamic.
Article Snippet: The following dataset was generated: Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 RCSB Protein Data Bank 7V4H Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly RCSB Protein Data Bank 7V4I Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I RCSB Protein Data Bank 7V4J Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II RCSB Protein Data Bank 7V4K Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III RCSB Protein Data Bank 7V4L
Techniques: Cryo-EM Sample Prep, Isolation