7EF7

Crystal Structure of Xanthosine monophosphate phosphatase complex with XMP

7EF7 の概要

• エントリーDOI: 10.2210/pdb7ef7/pdb
• 分子名称: At2g32150/F22D22.10, MAGNESIUM ION, XANTHOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: xmpase, hydrolase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28220.45

構造登録者

Yang, S.,Rhee, S. (登録日: 2021-03-21, 公開日: 2021-11-03, 最終更新日: 2023-11-29)

主引用文献

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

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: 34824243
DOI: 10.1038/s41467-021-27152-4

実験手法

X-RAY DIFFRACTION (1.5 Å)