7v4h: Difference between revisions
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The | ==Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2== | ||
<StructureSection load='7v4h' size='340' side='right'caption='[[7v4h]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4h OCA], [https://pdbe.org/7v4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4h RCSB], [https://www.ebi.ac.uk/pdbsum/7v4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4h ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme.,Chen Y, Xu W, Yu S, Ni K, She G, Ye X, Xing Q, Zhao J, Huang C Elife. 2021 Dec 13;10. pii: 72535. doi: 10.7554/eLife.72535. PMID:34898426<ref>PMID:34898426</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7v4h" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Xu | *[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chen Y]] | |||
[[Category: Huang C]] | |||
[[Category: Xing Q]] | |||
[[Category: Xu W]] | |||
Latest revision as of 08:15, 12 June 2024
Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2
Structural highlights
Publication Abstract from PubMedNature 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. Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme.,Chen Y, Xu W, Yu S, Ni K, She G, Ye X, Xing Q, Zhao J, Huang C Elife. 2021 Dec 13;10. pii: 72535. doi: 10.7554/eLife.72535. PMID:34898426[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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