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| | <StructureSection load='5tr2' size='340' side='right'caption='[[5tr2]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5tr2' size='340' side='right'caption='[[5tr2]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tr2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TR2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TR2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tr2]] 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=5TR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TR2 FirstGlance]. <br> |
| - | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5epc|5epc]], [[5f9c|5f9c]], [[5hsh|5hsh]], [[5jn5|5jn5]]</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=5tr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tr2 OCA], [https://pdbe.org/5tr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tr2 RCSB], [https://www.ebi.ac.uk/pdbsum/5tr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tr2 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/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tr2 OCA], [http://pdbe.org/5tr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tr2 RCSB], [http://www.ebi.ac.uk/pdbsum/5tr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tr2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/PGM1_HUMAN PGM1_HUMAN]] PGM-CDG;Glycogen storage disease due to phosphoglucomutase deficiency. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/PGM1_HUMAN PGM1_HUMAN] PGM-CDG;Glycogen storage disease due to phosphoglucomutase deficiency. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PGM1_HUMAN PGM1_HUMAN]] This enzyme participates in both the breakdown and synthesis of glucose. | + | [https://www.uniprot.org/uniprot/PGM1_HUMAN PGM1_HUMAN] This enzyme participates in both the breakdown and synthesis of glucose. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoglucomutase]]
| + | [[Category: Beamer LJ]] |
| - | [[Category: Beamer, L J]] | + | [[Category: Stiers KM]] |
| - | [[Category: Stiers, K M]] | + | |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Phosphohexomutase]]
| + | |
| Structural highlights
Disease
PGM1_HUMAN PGM-CDG;Glycogen storage disease due to phosphoglucomutase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
Function
PGM1_HUMAN This enzyme participates in both the breakdown and synthesis of glucose.
Publication Abstract from PubMed
The enzyme phosphoglucomutase 1 (PGM1) plays a central role in glucose homeostasis. Clinical studies have identified mutations in human PGM1 as the cause of PGM1 deficiency, an inherited metabolic disease. One residue, Asp263, has two known variants associated with disease: D263G and D263Y. Biochemical studies have shown that these mutants are soluble and well folded, but have significant catalytic impairment. To better understand this catalytic defect, we determined crystal structures of these two missense variants, both of which reveal a similar and indirect structural change due to the loss of a conserved salt bridge between Asp263 and Arg293. The arginine reorients into the active site, making interactions with residues responsible for substrate binding. Biochemical studies also show that the catalytic phosphoserine of the missense variants is more stable to hydrolysis relative to wild-type enzyme. The structural perturbation resulting from mutation of this single amino acid reveals the molecular mechanism underlying PGM1 deficiency in these missense variants. DATABASE: Structural data are available in the PDB under the accession numbers 5JN5 and 5TR2.
Asp263 missense variants perturb the active site of human phosphoglucomutase 1.,Stiers KM, Graham AC, Kain BN, Beamer LJ FEBS J. 2017 Jan 24. doi: 10.1111/febs.14025. PMID:28117557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stiers KM, Graham AC, Kain BN, Beamer LJ. Asp263 missense variants perturb the active site of human phosphoglucomutase 1. FEBS J. 2017 Jan 24. doi: 10.1111/febs.14025. PMID:28117557 doi:http://dx.doi.org/10.1111/febs.14025
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