6ypo

Arabidopsis aspartate transcarbamoylase bound to UMP

spinqualitylabelsall models 6ypo, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ypo is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: GOL, U5P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PYRB_ARATH 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate carbamoyltransferase 3D structures

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