1f5s

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(New page: 200px<br /><applet load="1f5s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5s, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''<br />
'''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''<br />
==Overview==
==Overview==
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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.
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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==
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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].
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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]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Jancarik, J.]]
[[Category: Jancarik, J.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:14 2008''

Revision as of 10:35, 21 February 2008


1f5s, resolution 1.8Å

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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 with and as ligands. Active as Phosphoserine phosphatase, with EC number 3.1.3.3 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

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