Summary for 1B0J
| Entry DOI | 10.2210/pdb1b0j/pdb |
| Descriptor | ACONITATE HYDRATASE, IRON/SULFUR CLUSTER, ISOCITRIC ACID, ... (4 entities in total) |
| Functional Keywords | lyase, complex, transit peptide |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 83333.84 |
| Authors | Lloyd, S.J.,Lauble, H.,Prasad, G.S.,Stout, C.D. (deposition date: 1998-11-10, release date: 1998-11-18, Last modification date: 2023-08-09) |
| Primary citation | Lloyd, S.J.,Lauble, H.,Prasad, G.S.,Stout, C.D. The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex Protein Sci., 8:2655-2662, 1999 Cited by PubMed Abstract: The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism. PubMed: 10631981PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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