1F5S

CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII

1F5S の概要

• エントリーDOI: 10.2210/pdb1f5s/pdb
• 分子名称: PHOSPHOSERINE PHOSPHATASE (PSP), PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: nad(p)-binding rossmann fold, four helix bundle, beta-hair pin, had family hydrolase, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47697.81

構造登録者

Wang, W.,Kim, R.,Jancarik, J.,Yokota, H.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (登録日: 2000-06-15, 公開日: 2001-06-20, 最終更新日: 2024-03-13)

主引用文献

Wang, W.,Kim, R.,Jancarik, J.,Yokota, H.,Kim, S.H.
Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution.
Structure, 9:65-72, 2001

PubMed Abstract: D-Serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate receptors, a major neurotransmitter receptor family in mammalian nervous systems. D-Serine is converted from L-serine, 90% of which is the product of the enzyme phosphoserine phosphatase (PSP). PSP from M. jannaschii (MJ) shares significant sequence homology with human PSP. PSPs and P-type ATPases are members of the haloacid dehalogenase (HAD)-like hydrolase family, and all members share three conserved sequence motifs. PSP and P-type ATPases utilize a common mechanism that involves Mg(2+)-dependent phosphorylation and autodephosphorylation at an aspartyl side chain in the active site. The strong resemblance in sequence and mechanism implies structural similarity among these enzymes.

PubMed: 11342136
DOI: 10.1016/S0969-2126(00)00558-X

実験手法

X-RAY DIFFRACTION (1.8 Å)