Summary for 6PX2
| Entry DOI | 10.2210/pdb6px2/pdb |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | complex with nad, oxidoreductase |
| Biological source | Acropora millepora (Staghorn coral) |
| Total number of polymer chains | 8 |
| Total formula weight | 317675.79 |
| Authors | Brandt, G.S.,Fields, P.A. (deposition date: 2019-07-24, release date: 2019-12-25, Last modification date: 2024-01-17) |
| Primary citation | Perez, A.M.,Wolfe, J.A.,Schermerhorn, J.T.,Qian, Y.,Cela, B.A.,Kalinowski, C.R.,Largoza, G.E.,Fields, P.A.,Brandt, G.S. Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coral Acropora millepora. Rsc Adv, 11:10364-10374, 2021 Cited by PubMed Abstract: Corals are vulnerable to increasing ocean temperatures. It is known that elevated temperatures lead to the breakdown of an essential mutualistic relationship with photosynthetic algae. The molecular mechanisms of this temperature-dependent loss of symbiosis are less well understood. Here, the thermal stability of a critical metabolic enzyme, glyceraldehyde-3-phosphate dehydrogenase, from the stony coral was found to increase significantly in the presence of its cofactor NAD. Determination of the structure of the cofactor-enzyme complex (PDB ID 6PX2) revealed variable NAD occupancy across the four monomers of the tetrameric enzyme. The structure of the fully occupied monomers was compared to those with partial cofactor occupancy, identifying regions of difference that may account for the increased thermal stability. PubMed: 35423531DOI: 10.1039/d0ra10119b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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