7evt: Difference between revisions

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-'''Unreleased structure'''
-The entry 7evt is ON HOLD
+==Crystal structure of the N-terminal degron-truncated human glutamine synthetase==
+<StructureSection load='7evt' size='340' side='right'caption='[[7evt]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7evt]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EVT FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#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=7evt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7evt OCA], [https://pdbe.org/7evt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7evt RCSB], [https://www.ebi.ac.uk/pdbsum/7evt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7evt ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/GLNA_HUMAN GLNA_HUMAN] Defects in GLUL are the cause of congenital systemic glutamine deficiency (CSGD) [MIM:[https://omim.org/entry/610015 610015]. CSGD is a rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid.<ref>PMID:16267323</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/GLNA_HUMAN GLNA_HUMAN] This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.<ref>PMID:18662667</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Glutamine synthetase (GS) is a decameric enzyme that plays a key role in nitrogen metabolism. Acetylation of the N-terminal degron (N-degron) of GS is essential for ubiquitylation and subsequent GS degradation. The full-length GS structure showed that the N-degron is buried inside the GS decamer and is inaccessible to the acetyltransferase. The structure of N-degron-truncated GS reported here reveals that the N-degron is not essential for GS decamer formation. It is also shown that the N-degron can be exposed to a solvent region through a series of conformational adjustments upon ligand binding. In summary, this study elucidated the dynamic movement of the N-degron and the possible effect of glutamine in enhancing the acetylation process.
-Authors:
+Crystal structure of N-terminal degron-truncated human glutamine synthetase.,Chek MF, Kim SY, Mori T, Kojima H, Hakoshima T Acta Crystallogr F Struct Biol Commun. 2021 Nov 1;77(Pt 11):427-434. doi:, 10.1107/S2053230X21010748. Epub 2021 Oct 29. PMID:34726182<ref>PMID:34726182</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7evt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chek MF]]
+[[Category: Hakoshima T]]
+[[Category: Kim SY]]
+[[Category: Mori T]]