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| | <StructureSection load='6y8x' size='340' side='right'caption='[[6y8x]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='6y8x' size='340' side='right'caption='[[6y8x]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6y8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atlantic_herring Atlantic herring]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y8X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y8X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clupea_harengus Clupea harengus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y8X 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=NA:SODIUM+ION'>NA</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]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6y8z|6y8z]], [[6y8y|6y8y]]</div></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=NA:SODIUM+ION'>NA</scene></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=6y8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y8x OCA], [http://pdbe.org/6y8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y8x RCSB], [http://www.ebi.ac.uk/pdbsum/6y8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y8x ProSAT]</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=6y8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y8x OCA], [https://pdbe.org/6y8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y8x RCSB], [https://www.ebi.ac.uk/pdbsum/6y8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y8x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atlantic herring]] | + | [[Category: Clupea harengus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eckhard, U]] | + | [[Category: Eckhard U]] |
| - | [[Category: Gustafsson, R]] | + | [[Category: Gustafsson R]] |
| - | [[Category: Selmer, M]] | + | [[Category: Selmer M]] |
| - | [[Category: Aciculin]]
| + | |
| - | [[Category: Binding partner]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Low to no activity]]
| + | |
| - | [[Category: Phosphoglucomutase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Phosphoglucomutase 5 (PGM5) in humans is known as a structural muscle protein without enzymatic activity, but detailed understanding of its function is lacking. PGM5 belongs to the alpha-D-phosphohexomutase family and is closely related to the enzymatically active metabolic enzyme PGM1. In the Atlantic herring, Clupea harengus, PGM5 is one of the genes strongly associated with ecological adaptation to the brackish Baltic Sea. We here present the first crystal structures of PGM5, from the Atlantic and Baltic herring, differing by a single substitution Ala330Val. The structure of PGM5 is overall highly similar to structures of PGM1. The structure of the Baltic herring PGM5 in complex with the substrate glucose-1-phosphate shows conserved substrate binding and active site compared to human PGM1, but both PGM5 variants lack phosphoglucomutase activity under the tested conditions. Structure comparison and sequence analysis of PGM5 and PGM1 from fish and mammals suggest that the lacking enzymatic activity of PGM5 is related to differences in active-site loops that are important for flipping of the reaction intermediate. The Ala330Val substitution does not alter structure or biophysical properties of PGM5 but, due to its surface-exposed location, could affect interactions with protein-binding partners.
Structure and Characterization of Phosphoglucomutase 5 from Atlantic and Baltic Herring-An Inactive Enzyme with Intact Substrate Binding.,Gustafsson R, Eckhard U, Ye W, Enbody ED, Pettersson M, Jemth P, Andersson L, Selmer M Biomolecules. 2020 Dec 3;10(12). pii: biom10121631. doi: 10.3390/biom10121631. PMID:33287293[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gustafsson R, Eckhard U, Ye W, Enbody ED, Pettersson M, Jemth P, Andersson L, Selmer M. Structure and Characterization of Phosphoglucomutase 5 from Atlantic and Baltic Herring-An Inactive Enzyme with Intact Substrate Binding. Biomolecules. 2020 Dec 3;10(12). pii: biom10121631. doi: 10.3390/biom10121631. PMID:33287293 doi:http://dx.doi.org/10.3390/biom10121631
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