1f5s
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1f5s.gif|left|200px]] | [[Image:1f5s.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1f5s", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1f5s| PDB=1f5s | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII''' | '''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII''' | ||
Line 32: | Line 29: | ||
[[Category: Wang, W.]] | [[Category: Wang, W.]] | ||
[[Category: Yokota, H.]] | [[Category: Yokota, H.]] | ||
- | [[Category: | + | [[Category: Berkeley structural genomics center]] |
- | [[Category: | + | [[Category: Beta-hair pin]] |
- | [[Category: | + | [[Category: Bsgc structure funded by nih]] |
- | [[Category: | + | [[Category: Four helix bundle]] |
- | [[Category: | + | [[Category: Had family hydrolase]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | + | [[Category: Psi]] | |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:56:10 2008'' |
- | + | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 12:56, 2 May 2008
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 Fri May 2 15:56:10 2008
Categories: 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 | Protein structure initiative | Psi | Structural genomic