1f5s | pdb_00001f5s
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| 1f5s, resolution 1.8Å | |||||||||||||
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| Ligands: | MG, PO4 | ||||||||||||
| Activity: | Phosphoserine phosphatase, with EC number 3.1.3.3 | ||||||||||||
| Domains: | SerB | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII
Overview
BACKGROUND: 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. RESULTS: The PSP crystal structure resembles the NAD(P) binding Rossmann fold with a large insertion of a four-helix-bundle domain and a beta hairpin. Three known conserved sequence motifs are arranged next to each other in space and outline the active site. A phosphate and a magnesium ion are bound to the active site. The active site is within a closed environment between the core alpha/beta domain and the four-helix-bundle domain. CONCLUSIONS: The crystal structure of MJ PSP was determined at 1.8 A resolution. Critical residues were assigned based on the active site structure and ligand binding geometry. The PSP structure is in a closed conformation that may resemble the phosphoserine bound state or the state after autodephosphorylation. Compared to a P-type ATPase (Ca(2+)-ATPase) structure, which is in an open state, this PSP structure appears also to be a good model for the closed conformation of P-type ATPase.
About this Structure
1F5S is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution., Wang W, Kim R, Jancarik J, Yokota H, Kim SH, Structure. 2001 Jan 10;9(1):65-71. PMID:11342136
Page seeded by OCA on Wed Mar 26 05:52:19 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Methanocaldococcus jannaschii
- Phosphoserine phosphatase
- Single protein
- BSGC, Berkeley Structural Genomics Center.
- Jancarik, J.
- Kim, R.
- Kim, S H.
- Wang, W.
- Yokota, H.
- Berkeley structural genomics center
- Beta-hair pin
- Bsgc structure funded by nih
- Four helix bundle
- Had family hydrolase
- Nad(p)-binding rossmann fold
- Protein structure initiative
- Psi
- Structural genomic
