5TVO
Crystal structure of Trypanosoma brucei AdoMetDC-delta26 monomer
Summary for 5TVO
| Entry DOI | 10.2210/pdb5tvo/pdb |
| Related | 5TVF 5TVM |
| Descriptor | S-adenosylmethionine decarboxylase proenzyme, PYRUVIC ACID, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | autoinhibition, cis-proline, lyase |
| Biological source | Trypanosoma brucei brucei (strain 927/4 GUTat10.1) More |
| Total number of polymer chains | 2 |
| Total formula weight | 38865.65 |
| Authors | Volkov, O.A.,Ariagno, C.,Chen, Z.,Tomchick, D.R.,Phillips, M.A. (deposition date: 2016-11-09, release date: 2016-12-28, Last modification date: 2024-03-13) |
| Primary citation | Volkov, O.A.,Kinch, L.N.,Ariagno, C.,Deng, X.,Zhong, S.,Grishin, N.V.,Tomchick, D.R.,Chen, Z.,Phillips, M.A. Relief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralog. Elife, 5:-, 2016 Cited by PubMed Abstract: Catalytically inactive enzyme paralogs occur in many genomes. Some regulate their active counterparts but the structural principles of this regulation remain largely unknown. We report X-ray structures of -adenosylmethionine decarboxylase alone and in functional complex with its catalytically dead paralogous partner, prozyme. We show monomeric AdoMetDC is inactive because of autoinhibition by its N-terminal sequence. Heterodimerization with prozyme displaces this sequence from the active site through a complex mechanism involving a -to- proline isomerization, reorganization of a β-sheet, and insertion of the N-terminal α-helix into the heterodimer interface, leading to enzyme activation. We propose that the evolution of this intricate regulatory mechanism was facilitated by the acquisition of the dimerization domain, a single step that can in principle account for the divergence of regulatory schemes in the AdoMetDC enzyme family. These studies elucidate an allosteric mechanism in an enzyme and a plausible scheme by which such complex cooperativity evolved. PubMed: 27977001DOI: 10.7554/eLife.20198 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.481 Å) |
Structure validation
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