7v4j: Difference between revisions
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==Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I== | ==Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I== | ||
<StructureSection load='7v4j' size='340' side='right'caption='[[7v4j]]' scene=''> | <StructureSection load='7v4j' size='340' side='right'caption='[[7v4j]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4J FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4J FirstGlance]. <br> | ||
</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=7v4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4j OCA], [https://pdbe.org/7v4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4j RCSB], [https://www.ebi.ac.uk/pdbsum/7v4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4j ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=7v4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4j OCA], [https://pdbe.org/7v4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4j RCSB], [https://www.ebi.ac.uk/pdbsum/7v4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4j ProSAT]</span></td></tr> | |||
</table> | </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> | |||
</div> | |||
<div class="pdbe-citations 7v4j" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 08:15, 12 June 2024
Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State ICryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I
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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