7v4l: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III==
-<StructureSection load='7v4l' size='340' side='right'caption='[[7v4l]]' scene=''>
+<StructureSection load='7v4l' size='340' side='right'caption='[[7v4l]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4L 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=7v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4l OCA], [https://pdbe.org/7v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4l RCSB], [https://www.ebi.ac.uk/pdbsum/7v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4l 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]] 3.4&#8491;</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=7v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4l OCA], [https://pdbe.org/7v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4l RCSB], [https://www.ebi.ac.uk/pdbsum/7v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4l 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7v4l" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>