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<StructureSection load='1f5s' size='340' side='right'caption='[[1f5s]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1f5s' size='340' side='right'caption='[[1f5s]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5S FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5s OCA], [https://pdbe.org/1f5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5s RCSB], [https://www.ebi.ac.uk/pdbsum/1f5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5s ProSAT], [https://www.topsan.org/Proteins/BSGC/1f5s TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5s OCA], [https://pdbe.org/1f5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5s RCSB], [https://www.ebi.ac.uk/pdbsum/1f5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5s ProSAT], [https://www.topsan.org/Proteins/BSGC/1f5s TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SERB_METJA SERB_METJA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f5s ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f5s ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11342136</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f5s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphoserine phosphatase|Phosphoserine phosphatase]]
*[[Phosphoserine phosphatase|Phosphoserine phosphatase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphoserine phosphatase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Structural genomic]]
[[Category: Jancarik J]]
[[Category: Jancarik, J]]
[[Category: Kim R]]
[[Category: Kim, R]]
[[Category: Kim SH]]
[[Category: Kim, S H]]
[[Category: Wang W]]
[[Category: Wang, W]]
[[Category: Yokota H]]
[[Category: Yokota, H]]
[[Category: Beta-hair pin]]
[[Category: Bsgc structure funded by nih]]
[[Category: Four helix bundle]]
[[Category: Had family hydrolase]]
[[Category: Hydrolase]]
[[Category: PSI, Protein structure initiative]]

Latest revision as of 13:23, 13 March 2024

CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII

1f5s, resolution 1.80Å

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