Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis

Hsing Mao Chu, Rey Ting Guo, Ting Wan Lin, Chia Cheng Chou, Hui Lin Shr, Hui Lin Lai, Tsung Yin Tang, Kuo Joan Cheng, Brent L. Selinger, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

84 Citations (Scopus)

Abstract

Various inositide phosphatases participate in the regulation of inositol polyphosphate signaling molecules. Plant phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and phosphate. The phytase from Selenomonas ruminantium shares no sequence homology with other microbial phytases. Its crystal structure revealed a phytase fold of the dual-specificity phosphatase type. The active site is located near a conserved cysteine-containing (Cys241) P loop. We also solved two other crystal forms in which an inhibitor, myo-inositol hexasulfate, is cocrystallized with the enzyme. In the "standby" and the "inhibited" crystal forms, the inhibitor is bound, respectively, in a pocket slightly away from Cys241 and at the substrate binding site where the phosphate group to be hydrolyzed is held close to the -SH group of Cys241. Our structural and mutagenesis studies allow us to visualize the way in which the P loop-containing phytase attracts and hydrolyzes the substrate (phytate) sequentially.

Original languageEnglish
Pages (from-to)2015-2024
Number of pages10
JournalStructure
Volume12
Issue number11
DOIs
Publication statusPublished - Nov 2004
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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