6Y8Z
Structure of Baltic Herring (Clupea Harengus) Phosphoglucomutase 5 (PGM5)
Summary for 6Y8Z
| Entry DOI | 10.2210/pdb6y8z/pdb |
| Related | 6Y8X 6Y8Y |
| Descriptor | Phosphoglucomutase 5, NICKEL (II) ION, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | phosphoglucomutase, aciculin, binding partner, low to no activity, isomerase |
| Biological source | Clupea harengus |
| Total number of polymer chains | 1 |
| Total formula weight | 65648.03 |
| Authors | Gustafsson, R.,Eckhard, U.,Selmer, M. (deposition date: 2020-03-06, release date: 2020-12-16, Last modification date: 2024-01-24) |
| Primary citation | Gustafsson, R.,Eckhard, U.,Ye, W.,Enbody, E.D.,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, 10:-, 2020 Cited by PubMed Abstract: 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, , 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. PubMed: 33287293DOI: 10.3390/biom10121631 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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