5TS9
Crystal structure of Chorismate mutase from Burkholderia phymatum
Summary for 5TS9
| Entry DOI | 10.2210/pdb5ts9/pdb |
| Descriptor | Chorismate mutase (2 entities in total) |
| Functional Keywords | ssgcid, chorismate mutase, burkholderia phymatum, structural genomics, seattle structural genomics center for infectious disease, isomerase |
| Biological source | Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) |
| Total number of polymer chains | 8 |
| Total formula weight | 150401.22 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2016-10-28, release date: 2016-11-23, Last modification date: 2024-10-23) |
| Primary citation | Asojo, O.A.,Subramanian, S.,Abendroth, J.,Exley, I.,Lorimer, D.D.,Edwards, T.E.,Myler, P.J. Crystal structure of chorismate mutase from Burkholderia phymatum. Acta Crystallogr F Struct Biol Commun, 74:187-192, 2018 Cited by PubMed Abstract: The bacterium Burkholderia phymatum is a promiscuous symbiotic nitrogen-fixating bacterium that belongs to one of the largest groups of Betaproteobacteria. Other Burkholderia species are known to cause disease in plants and animals, and some are potential agents for biological warfare. Structural genomics efforts include characterizing the structures of enzymes from pathways that can be targeted for drug development. As part of these efforts, chorismate mutase from B. phymatum was produced and crystallized, and a 1.95 Å resolution structure is reported. This enzyme shares less than 33% sequence identity with other homologs of known structure. There are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQγ has reported roles in virulence. Chorismate mutase from B. phymatum has the prototypical AroQγ topology and retains the characteristic chorismate mutase active site. This suggests that substrate-based chorismate mutase inhibitors will not be specific and are likely to affect beneficial bacteria such as B. phymatum. PubMed: 29633965DOI: 10.1107/S2053230X18002868 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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