6yvb: Difference between revisions
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==Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate== | |||
<StructureSection load='6yvb' size='340' side='right'caption='[[6yvb]], [[Resolution|resolution]] 1.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6yvb]] is a 6 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=6YVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YVB 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]] 1.826Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=6yvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yvb OCA], [https://pdbe.org/6yvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yvb RCSB], [https://www.ebi.ac.uk/pdbsum/6yvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yvb ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6yvb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Bellin L]] | |||
[[Category: Del Cano Ochoa F]] | |||
[[Category: Mohlmann T]] | |||
[[Category: Ramon Maiques S]] | |||
Latest revision as of 16:36, 24 January 2024
Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphateArabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate
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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