2HKI
Crystal structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase A4 isoform
Summary for 2HKI
| Entry DOI | 10.2210/pdb2hki/pdb |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase A, chloroplast, SULFATE ION (2 entities in total) |
| Functional Keywords | rossmann fold, apo-form, oxidoreductase |
| Biological source | Spinacia oleracea (spinach) |
| Cellular location | Plastid, chloroplast: P19866 |
| Total number of polymer chains | 1 |
| Total formula weight | 36640.64 |
| Authors | Camara-Artigas, A. (deposition date: 2006-07-04, release date: 2006-11-14, Last modification date: 2023-08-30) |
| Primary citation | Camara-Artigas, A.,Hirasawa, M.,Knaff, D.B.,Wang, M.,Allen, J.P. Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form. Acta Crystallogr.,Sect.F, 62:1087-1092, 2006 Cited by PubMed Abstract: Two crystalline forms of GADPH (D-glyceraldehyde-3-phosphate dehydrogenase) from Spinacia oleracea were obtained using sitting-drop vapor diffusion. Despite the very low concentration of GADPH in the solutions, two crystalline forms were obtained, one of which was the previously reported C222 space group with unit-cell parameters a = 155.3, b = 181.7, c = 107.6 A and the other of which belonged to a new space group I4(1)22, with unit-cell parameters a = b = 120.9, c = 154.5 A. Diffraction data were measured from both native and derivatives, yielding structures at a resolution limit of 3.0 A. Differences at the NAD(+)/NADP(+)-binding site seen in these structures compared with the previously reported structure with bound coenzyme suggest that conformational changes associated with pyridine-nucleotide binding may play a role in the regulation of this enzyme. PubMed: 17077485DOI: 10.1107/S174430910604200X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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