View source for 5u05


==Cryo-EM structure of the E. coli CTP synthase tetramer==
<SX load='5u05' size='340' side='right' viewer='molstar' caption='[[5u05]], [[Resolution|resolution]] 7.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5u05]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U05 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]] 7.9&#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=5u05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u05 OCA], [https://pdbe.org/5u05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u05 RCSB], [https://www.ebi.ac.uk/pdbsum/5u05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u05 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/PYRG_ECOLI PYRG_ECOLI] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.[HAMAP-Rule:MF_01227]
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== Publication Abstract from PubMed ==
The universally conserved enzyme CTP synthase (CTPS) forms filaments in bacteria and eukaryotes. In bacteria, polymerization inhibits CTPS activity and is required for nucleotide homeostasis. Here we show that for human CTPS, polymerization increases catalytic activity. The cryo-EM structures of bacterial and human CTPS filaments differ considerably in overall architecture and in the conformation of the CTPS protomer, explaining the divergent consequences of polymerization on activity. The structure of human CTPS filament, the first structure of the full-length human enzyme, reveals a novel active conformation. The filament structures elucidate allosteric mechanisms of assembly and regulation that rely on a conserved conformational equilibrium. The findings may provide a mechanism for increasing human CTPS activity in response to metabolic state and challenge the assumption that metabolic filaments are generally storage forms of inactive enzymes. Allosteric regulation of CTPS polymerization by ligands likely represents a fundamental mechanism underlying assembly of other metabolic filaments.

Human CTP synthase filament structure reveals the active enzyme conformation.,Lynch EM, Hicks DR, Shepherd M, Endrizzi JA, Maker A, Hansen JM, Barry RM, Gitai Z, Baldwin EP, Kollman JM Nat Struct Mol Biol. 2017 May 1. doi: 10.1038/nsmb.3407. PMID:28459447<ref>PMID:28459447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5u05" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Hicks DR]]
[[Category: Kollman JM]]
[[Category: Lynch EM]]