View source for 1nnl


==Crystal structure of Human Phosphoserine Phosphatase==
<StructureSection load='1nnl' size='340' side='right'caption='[[1nnl]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nnl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NNL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f5s|1f5s]], [[1j97|1j97]], [[1l7m|1l7m]], [[1l7n|1l7n]], [[1l7o|1l7o]], [[1l7p|1l7p]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nnl OCA], [http://pdbe.org/1nnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nnl RCSB], [http://www.ebi.ac.uk/pdbsum/1nnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nnl ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>  
== Function ==
[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>  
== 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/nn/1nnl_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=1nnl ConSurf].
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== Publication Abstract from PubMed ==
The crystal structure of human phosphoserine phosphatase (HPSP) in the open conformation has been determined at a resolution of 1.53 A. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03, b = 130.25, c = 157.29 A. The asymmetric unit contains two molecules. Phase information was derived from a multiwavelength anomalous dispersion (MAD) experiment conducted at three wavelengths using a selenomethionine-derivative crystal of HPSP. The structure was refined using CNS to a final crystallographic R value of 21.6% (R(free) = 23.4%). HPSP is a dimeric enzyme responsible for the third and final step of the l-serine biosynthesis pathway. It catalyses the Mg2+-dependent hydrolysis of l-phosphoserine. Recently, the structure of HPSP in complex with an inhibitor bound to the active site has been reported to be the open conformation of the enzyme. Here, the structure of HPSP is reported in the absence of substrate in the active site. Evidence is presented that HPSP in an uncomplexed form is in an even more open conformation than in the inhibitor complex. In this state, the enzyme is partially unfolded to allow the substrate to enter the active site. Binding of the substrate causes HPSP to shift to the closed conformation by stabilizing the partially unfolded region. In the present structure a Ca2+ ion is bound to the active site and an explanation is given why HPSP is not active when in the active site Mg2+ is replaced by a Ca2+ ion.

High-resolution structure of human phosphoserine phosphatase in open conformation.,Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):971-7. Epub 2003, May 23. PMID:12777757<ref>PMID:12777757</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Phosphoserine phosphatase|Phosphoserine phosphatase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Phosphoserine phosphatase]]
[[Category: Collet, J F]]
[[Category: Peeraer, Y]]
[[Category: Rabijns, A]]
[[Category: Ranter, C De]]
[[Category: Schaftingen, E Van]]
[[Category: Verboven, C]]
[[Category: Hpsp]]
[[Category: Hydrolase]]
[[Category: Phospho-aspartyl]]
[[Category: Psp]]