4FDT

Crystal Structure of a Multiple Inositol Polyphosphate Phosphatase

4FDT の概要

• エントリーDOI: 10.2210/pdb4fdt/pdb
• 関連するPDBエントリー: 4FDU
• 分子名称: Putative multiple inositol polyphosphate histidine phosphatase 1, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: phosphatase, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98720.93

構造登録者

Li, A.W.H.,Hemmings, A.M. (登録日: 2012-05-29, 公開日: 2014-01-29, 最終更新日: 2024-02-28)

主引用文献

Stentz, R.,Osborne, S.,Horn, N.,Li, A.W.,Hautefort, I.,Bongaerts, R.,Rouyer, M.,Bailey, P.,Shears, S.B.,Hemmings, A.M.,Brearley, C.A.,Carding, S.R.
A Bacterial Homolog of a Eukaryotic Inositol Phosphate Signaling Enzyme Mediates Cross-kingdom Dialog in the Mammalian Gut.
Cell Rep, 6:646-656, 2014

PubMed Abstract: Dietary InsP6 can modulate eukaryotic cell proliferation and has complex nutritive consequences, but its metabolism in the mammalian gastrointestinal tract is poorly understood. Therefore, we performed phylogenetic analyses of the gastrointestinal microbiome in order to search for candidate InsP6 phosphatases. We determined that prominent gut bacteria express homologs of the mammalian InsP6 phosphatase (MINPP) and characterized the enzyme from Bacteroides thetaiotaomicron (BtMinpp). We show that BtMinpp has exceptionally high catalytic activity, which we rationalize on the basis of mutagenesis studies and by determining its crystal structure at 1.9 Å resolution. We demonstrate that BtMinpp is packaged inside outer membrane vesicles (OMVs) protecting the enzyme from degradation by gastrointestinal proteases. Moreover, we uncover an example of cross-kingdom cell-to-cell signaling, showing that the BtMinpp-OMVs interact with intestinal epithelial cells to promote intracellular Ca(2+) signaling. Our characterization of BtMinpp offers several directions for understanding how the microbiome serves human gastrointestinal physiology.

PubMed: 24529702
DOI: 10.1016/j.celrep.2014.01.021

実験手法

X-RAY DIFFRACTION (1.93 Å)