3GTD
2.4 Angstrom crystal structure of fumarate hydratase from Rickettsia prowazekii
Summary for 3GTD
| Entry DOI | 10.2210/pdb3gtd/pdb |
| Descriptor | Fumarate hydratase class II, MALONATE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | structural genomics, ssgcid, fumarate, hydratase, lyase, tricarboxylic acid cycle, seattle structural genomics center for infectious disease |
| Biological source | Rickettsia prowazekii |
| Cellular location | Cytoplasm (By similarity): Q9ZCQ4 |
| Total number of polymer chains | 2 |
| Total formula weight | 106943.16 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-03-27, release date: 2009-07-14, Last modification date: 2023-09-06) |
| Primary citation | Phan, I.,Subramanian, S.,Olsen, C.,Edwards, T.E.,Guo, W.,Zhang, Y.,Van Voorhis, W.C.,Stewart, L.J.,Myler, P.J. Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria. Acta Crystallogr.,Sect.F, 67:1123-1128, 2011 Cited by PubMed Abstract: Rickettsiae are obligate intracellular parasites of eukaryotic cells that are the causative agents responsible for spotted fever and typhus. Their small genome (about 800 protein-coding genes) is highly conserved across species and has been postulated as the ancestor of the mitochondria. No genes that are required for glycolysis are found in the Rickettsia prowazekii or mitochondrial genomes, but a complete set of genes encoding components of the tricarboxylic acid cycle and the respiratory-chain complex is found in both. A 2.4 Å resolution crystal structure of R. prowazekii fumarate hydratase, an enzyme catalyzing the third step of the tricarboxylic acid cycle pathway that ultimately converts phosphoenolpyruvate into succinyl-CoA, has been solved. A structure alignment with human mitochondrial fumarate hydratase highlights the close similarity between R. prowazekii and mitochondrial enzymes. PubMed: 21904061DOI: 10.1107/S174430911102690X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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