6l6z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the Drosophila CTP synthase substrate-bound filament== | |
| + | <StructureSection load='6l6z' size='340' side='right'caption='[[6l6z]], [[Resolution|resolution]] 6.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6l6z]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L6Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CTP_synthase_(glutamine_hydrolyzing) CTP synthase (glutamine hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6l6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l6z OCA], [http://pdbe.org/6l6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l6z RCSB], [http://www.ebi.ac.uk/pdbsum/6l6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l6z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PYRG_DROME PYRG_DROME]] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides (By similarity). Isoform 1 is required for cytoophidium assembly in female germline cells.<ref>PMID:23459760</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Intracellular compartmentation is a key strategy for the functioning of a cell. In 2010, several studies revealed that the metabolic enzyme CTP synthase (CTPS) can form filamentous structures termed cytoophidia in prokaryotic and eukaryotic cells. However, recent structural studies showed that CTPS only forms inactive product-bound filaments in bacteria while forming active substrate-bound filaments in eukaryotic cells. In this study, using negative staining and cryo-electron microscopy, we demonstrate that Drosophila CTPS, whether in substrate-bound or product-bound form, can form filaments. Our results challenge the previous model and indicate that substrate-bound and product-bound filaments can coexist in the same species. We speculate that the ability to switch between active and inactive cytoophidia in the same cells provides an additional layer of metabolic regulation. | ||
| - | + | Drosophila CTP synthase can form distinct substrate- and product-bound filaments.,Zhou X, Guo CJ, Hu HH, Zhong J, Sun Q, Liu D, Zhou S, Chang CC, Liu JL J Genet Genomics. 2019 Nov 20;46(11):537-545. doi: 10.1016/j.jgg.2019.11.006., Epub 2019 Nov 29. PMID:31902586<ref>PMID:31902586</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6l6z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen-Jun, G]] | ||
| + | [[Category: Ji-Long, L]] | ||
| + | [[Category: Xian, Z]] | ||
| + | [[Category: Filament]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Substrate-bound]] | ||
Revision as of 09:40, 18 March 2020
Cryo-EM structure of the Drosophila CTP synthase substrate-bound filament
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