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==Arabidopsis aspartate transcarbamoylase complex with PALA== | ==Arabidopsis aspartate transcarbamoylase complex with PALA== | ||
<StructureSection load='6ys6' size='340' side='right'caption='[[6ys6]]' scene=''> | <StructureSection load='6ys6' size='340' side='right'caption='[[6ys6]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YS6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ys6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YS6 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=6ys6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ys6 OCA], [https://pdbe.org/6ys6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ys6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ys6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ys6 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6ys6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ys6 OCA], [https://pdbe.org/6ys6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ys6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ys6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ys6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PYRB_ARATH PYRB_ARATH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aspartate transcarbamoylase (ATC), an essential enzyme for de novo pyrimidine biosynthesis, is uniquely regulated in plants by feedback inhibition of uridine 5-monophosphate (UMP). Despite its importance in plant growth, the structure of this UMP-controlled ATC and the regulatory mechanism remain unknown. Here, we report the crystal structures of Arabidopsis ATC trimer free and bound to UMP, complexed to a transition-state analog or bearing a mutation that turns the enzyme insensitive to UMP. We found that UMP binds and blocks the ATC active site, directly competing with the binding of the substrates. We also prove that UMP recognition relies on a loop exclusively conserved in plants that is also responsible for the sequential firing of the active sites. In this work, we describe unique regulatory and catalytic properties of plant ATCs that could be exploited to modulate de novo pyrimidine synthesis and plant growth. | |||
Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase.,Bellin L, Del Cano-Ochoa F, Velazquez-Campoy A, Mohlmann T, Ramon-Maiques S Nat Commun. 2021 Feb 11;12(1):947. doi: 10.1038/s41467-021-21165-9. PMID:33574254<ref>PMID:33574254</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ys6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bellin L]] | [[Category: Bellin L]] | ||
Latest revision as of 16:34, 24 January 2024
Arabidopsis aspartate transcarbamoylase complex with PALAArabidopsis aspartate transcarbamoylase complex with PALA
Structural highlights
FunctionPublication Abstract from PubMedAspartate transcarbamoylase (ATC), an essential enzyme for de novo pyrimidine biosynthesis, is uniquely regulated in plants by feedback inhibition of uridine 5-monophosphate (UMP). Despite its importance in plant growth, the structure of this UMP-controlled ATC and the regulatory mechanism remain unknown. Here, we report the crystal structures of Arabidopsis ATC trimer free and bound to UMP, complexed to a transition-state analog or bearing a mutation that turns the enzyme insensitive to UMP. We found that UMP binds and blocks the ATC active site, directly competing with the binding of the substrates. We also prove that UMP recognition relies on a loop exclusively conserved in plants that is also responsible for the sequential firing of the active sites. In this work, we describe unique regulatory and catalytic properties of plant ATCs that could be exploited to modulate de novo pyrimidine synthesis and plant growth. Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase.,Bellin L, Del Cano-Ochoa F, Velazquez-Campoy A, Mohlmann T, Ramon-Maiques S Nat Commun. 2021 Feb 11;12(1):947. doi: 10.1038/s41467-021-21165-9. PMID:33574254[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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