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New page: left|200px<br /><applet load="1f5s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5s, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1f5s.gif|left|200px]]<br /><applet load="1f5s" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1f5s.gif|left|200px]]<br /><applet load="1f5s" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f5s, resolution 1.8&Aring;" />
caption="1f5s, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''<br />
'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''<br />


==Overview==
==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.
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==
==About this Structure==
1F5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with PO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F5S OCA].  
1F5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5S OCA].  


==Reference==
==Reference==
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[[Category: Phosphoserine phosphatase]]
[[Category: Phosphoserine phosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Jancarik, J.]]
[[Category: Jancarik, J.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
[[Category: Kim, S.H.]]
[[Category: Kim, S H.]]
[[Category: Wang, W.]]
[[Category: Wang, W.]]
[[Category: Yokota, H.]]
[[Category: Yokota, H.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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