7EF7
Crystal Structure of Xanthosine monophosphate phosphatase complex with XMP
Summary for 7EF7
| Entry DOI | 10.2210/pdb7ef7/pdb |
| Descriptor | At2g32150/F22D22.10, MAGNESIUM ION, XANTHOSINE-5'-MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | xmpase, hydrolase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 28220.45 |
| Authors | |
| Primary citation | Heinemann, K.J.,Yang, S.Y.,Straube, H.,Medina-Escobar, N.,Varbanova-Herde, M.,Herde, M.,Rhee, S.,Witte, C.P. Initiation of cytosolic plant purine nucleotide catabolism involves a monospecific xanthosine monophosphate phosphatase. Nat Commun, 12:6846-6846, 2021 Cited by PubMed Abstract: In plants, guanosine monophosphate (GMP) is synthesized from adenosine monophosphate via inosine monophosphate and xanthosine monophosphate (XMP) in the cytosol. It has been shown recently that the catabolic route for adenylate-derived nucleotides bifurcates at XMP from this biosynthetic route. Dephosphorylation of XMP and GMP by as yet unknown phosphatases can initiate cytosolic purine nucleotide catabolism. Here we show that Arabidopsis thaliana possesses a highly XMP-specific phosphatase (XMPP) which is conserved in vascular plants. We demonstrate that XMPP catalyzes the irreversible entry reaction of adenylate-derived nucleotides into purine nucleotide catabolism in vivo, whereas the guanylates enter catabolism via an unidentified GMP phosphatase and guanosine deaminase which are important to maintain purine nucleotide homeostasis. We also present a crystal structure and mutational analysis of XMPP providing a rationale for its exceptionally high substrate specificity, which is likely required for the efficient catalysis of the very small XMP pool in vivo. PubMed: 34824243DOI: 10.1038/s41467-021-27152-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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