1F5S

CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII

Summary for 1F5S

• Entry DOI: 10.2210/pdb1f5s/pdb
• Descriptor: PHOSPHOSERINE PHOSPHATASE (PSP), PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: 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
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 2
• Total formula weight: 47697.81

Authors

Wang, W.,Kim, R.,Jancarik, J.,Yokota, H.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2000-06-15, release date: 2001-06-20, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)