5nnq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Aspartate transcarbamoylase from Chaetomium thermophilum CAD-like bound to carbamoyl phosphate== | |
| + | <StructureSection load='5nnq' size='340' side='right' caption='[[5nnq]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5nnq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NNQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5nnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnq OCA], [http://pdbe.org/5nnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nnq RCSB], [http://www.ebi.ac.uk/pdbsum/5nnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CAD, the multifunctional protein initiating and controlling de novo biosynthesis of pyrimidines in animals, self-assembles into approximately 1.5 MDa hexamers. The structures of the dihydroorotase (DHO) and aspartate transcarbamoylase (ATC) domains of human CAD have been previously determined, but we lack information on how these domains associate and interact with the rest of CAD forming a multienzymatic unit. Here, we prove that a construct covering human DHO and ATC oligomerizes as a dimer of trimers and that this arrangement is conserved in CAD-like from fungi, which holds an inactive DHO-like domain. The crystal structures of the ATC trimer and DHO-like dimer from the fungus Chaetomium thermophilum confirm the similarity with the human CAD homologs. These results demonstrate that, despite being inactive, the fungal DHO-like domain has a conserved structural function. We propose a model that sets the DHO and ATC complex as the central element in the architecture of CAD. | ||
| - | + | Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis.,Moreno-Morcillo M, Grande-Garcia A, Ruiz-Ramos A, Del Cano-Ochoa F, Boskovic J, Ramon-Maiques S Structure. 2017 Jun 6;25(6):912-923.e5. doi: 10.1016/j.str.2017.04.012. Epub 2017, May 25. PMID:28552578<ref>PMID:28552578</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5nnq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Grande-Garcia, A]] | ||
| + | [[Category: Moreno-Morcillo, M]] | ||
| + | [[Category: Ramon-Maiques, S]] | ||
| + | [[Category: Cad]] | ||
| + | [[Category: Carbamoyl phosphate]] | ||
| + | [[Category: Transcarbamoylase superfamily]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Ura2]] | ||
Revision as of 11:34, 3 August 2017
Aspartate transcarbamoylase from Chaetomium thermophilum CAD-like bound to carbamoyl phosphate
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