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| [[Image:1f5s.gif|left|200px]]
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| {{Structure
| | ==CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII== |
| |PDB= 1f5s |SIZE=350|CAPTION= <scene name='initialview01'>1f5s</scene>, resolution 1.8Å
| | <StructureSection load='1f5s' size='340' side='right'caption='[[1f5s]], [[Resolution|resolution]] 1.80Å' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
| | <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> |
| |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>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| |GENE=
| | <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> |
| |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0560 SerB]</span>
| | <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> |
| |RELATEDENTRY=
| | </table> |
| |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>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/SERB_METJA SERB_METJA] |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/1f5s_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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> |
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| '''CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII'''
| | ==See Also== |
| | | *[[Phosphoserine phosphatase|Phosphoserine phosphatase]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| 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.
| | [[Category: Large Structures]] |
| | |
| ==About this Structure==
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| 1F5S is a [[Single protein]] structure of sequence from [http://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].
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| ==Reference==
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/11342136 11342136]
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| [[Category: Methanocaldococcus jannaschii]] | | [[Category: Methanocaldococcus jannaschii]] |
| [[Category: Phosphoserine phosphatase]]
| | [[Category: Jancarik J]] |
| [[Category: Single protein]]
| | [[Category: Kim R]] |
| [[Category: BSGC, Berkeley Structural Genomics Center.]]
| | [[Category: Kim SH]] |
| [[Category: Jancarik, J.]] | | [[Category: Wang W]] |
| [[Category: Kim, R.]] | | [[Category: Yokota H]] |
| [[Category: Kim, S H.]] | |
| [[Category: Wang, W.]] | |
| [[Category: Yokota, H.]] | |
| [[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: four helix bundle]]
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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: psi]]
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| [[Category: structural genomic]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:28 2008''
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