5BT9
Crystal Structure of FolM Alternative dihydrofolate reductase 1 from Brucella canis complexed with NADP
Summary for 5BT9
| Entry DOI | 10.2210/pdb5bt9/pdb |
| Descriptor | 3-oxoacyl-(Acyl-carrier-protein) reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | ssgcid, folm, alternative dihydrofolate reductase 1, fabg, oxidoreductase, structural genomics, seattle structural genomics center for infectious disease |
| Biological source | Brucella canis (strain ATCC 23365 / NCTC 10854) |
| Total number of polymer chains | 4 |
| Total formula weight | 122930.37 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2015-06-02, release date: 2015-07-29, Last modification date: 2025-10-22) |
| Primary citation | Porter, I.,Neal, T.,Walker, Z.,Hayes, D.,Fowler, K.,Billups, N.,Rhoades, A.,Smith, C.,Smith, K.,Staker, B.L.,Dranow, D.M.,Mayclin, S.J.,Subramanian, S.,Edwards, T.E.,Myler, P.J.,Asojo, O.A. Crystal structures of FolM alternative dihydrofolate reductase 1 from Brucella suis and Brucella canis. Acta Crystallogr.,Sect.F, 78:31-38, 2022 Cited by PubMed Abstract: Members of the bacterial genus Brucella cause brucellosis, a zoonotic disease that affects both livestock and wildlife. Brucella are category B infectious agents that can be aerosolized for biological warfare. As part of the structural genomics studies at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), FolM alternative dihydrofolate reductases 1 from Brucella suis and Brucella canis were produced and their structures are reported. The enzymes share ∼95% sequence identity but have less than 33% sequence identity to other homologues with known structure. The structures are prototypical NADPH-dependent short-chain reductases that share their highest tertiary-structural similarity with protozoan pteridine reductases, which are being investigated for rational therapeutic development. PubMed: 34981773DOI: 10.1107/S2053230X21013078 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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