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| | <StructureSection load='6hyj' size='340' side='right'caption='[[6hyj]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='6hyj' size='340' side='right'caption='[[6hyj]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hyj]] 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=6HYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hyj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HYJ 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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSPH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6hyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hyj OCA], [https://pdbe.org/6hyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hyj RCSB], [https://www.ebi.ac.uk/pdbsum/6hyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hyj ProSAT]</span></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=6hyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hyj OCA], [http://pdbe.org/6hyj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hyj RCSB], [http://www.ebi.ac.uk/pdbsum/6hyj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hyj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == 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> | + | [https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[https://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 == | | == 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> | + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6hyj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hyj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phosphoserine phosphatase|Phosphoserine phosphatase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoserine phosphatase]]
| + | [[Category: Haufroid M]] |
| - | [[Category: Haufroid, M]] | + | [[Category: Mirgaux M]] |
| - | [[Category: Mirgaux, M]] | + | [[Category: Wouters J]] |
| - | [[Category: Wouters, J]] | + | |
| - | [[Category: Homo sapien]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Disease
SERB_HUMAN Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:614023. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.[1]
Function
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.[2]
Publication Abstract from PubMed
The equilibrium between phosphorylation and dephosphorylation is one of the most important processes that takes place in living cells. Human phosphoserine phosphatase (hPSP) is a key enzyme in the production of serine by the dephosphorylation of phospho-L-serine. It is directly involved in the biosynthesis of other important metabolites such as glycine and D-serine (a neuromodulator). hPSP is involved in the survival mechanism of cancer cells and has recently been found to be an essential biomarker. Here, three new high-resolution crystal structures of hPSP (1.5-2.0 A) in complexes with phosphoserine and with serine, which are the substrate and the product of the reaction, respectively, and in complex with a noncleavable substrate analogue (homocysteic acid) are presented. New types of interactions take place between the enzyme and its ligands. Moreover, the loop involved in the open/closed state of the enzyme is fully refined in a totally unfolded conformation. This loop is further studied through molecular-dynamics simulations. Finally, all of these analyses allow a more complete reaction mechanism for this enzyme to be proposed which is consistent with previous publications on the subject.
Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase.,Haufroid M, Mirgaux M, Leherte L, Wouters J Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):592-604. doi:, 10.1107/S2059798319006867. Epub 2019 Jun 4. PMID:31205021[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E. Mutations responsible for 3-phosphoserine phosphatase deficiency. Eur J Hum Genet. 2004 Feb;12(2):163-6. PMID:14673469 doi:10.1038/sj.ejhg.5201083
- ↑ Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. High-resolution structure of human phosphoserine phosphatase in open conformation. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):971-7. Epub 2003, May 23. PMID:12777757
- ↑ Haufroid M, Mirgaux M, Leherte L, Wouters J. Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase. Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):592-604. doi:, 10.1107/S2059798319006867. Epub 2019 Jun 4. PMID:31205021 doi:http://dx.doi.org/10.1107/S2059798319006867
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