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1f5s

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[[Image:1f5s.gif|left|200px]]
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{{Structure
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|PDB= 1f5s |SIZE=350|CAPTION= <scene name='initialview01'>1f5s</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1f5s", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span>
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{{STRUCTURE_1f5s| PDB=1f5s | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5s OCA], [http://www.ebi.ac.uk/pdbsum/1f5s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f5s RCSB]</span>
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'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''
'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''
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[[Category: Wang, W.]]
[[Category: Wang, W.]]
[[Category: Yokota, H.]]
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[[Category: berkeley structural genomics center]]
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[[Category: Berkeley structural genomics center]]
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[[Category: beta-hair pin]]
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[[Category: bsgc structure funded by nih]]
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[[Category: Bsgc structure funded by nih]]
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[[Category: four helix bundle]]
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[[Category: Four helix bundle]]
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[[Category: had family hydrolase]]
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[[Category: Had family hydrolase]]
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[[Category: nad(p)-binding rossmann fold]]
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[[Category: Protein structure initiative]]
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[[Category: protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: structural genomic]]
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Revision as of 12:56, 2 May 2008

Image:1f5s.gif

Template:STRUCTURE 1f5s

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

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