2Y5J
Crystal structure of Burkholderia cenocepacia dihydropteroate synthase.
Summary for 2Y5J
| Entry DOI | 10.2210/pdb2y5j/pdb |
| Related | 2Y5S |
| Descriptor | DIHYDROPTEROATE SYNTHASE, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | transferase, folate biosynthesis |
| Biological source | BURKHOLDERIA CENOCEPACIA |
| Total number of polymer chains | 1 |
| Total formula weight | 31250.78 |
| Authors | Morgan, R.E.,Batot, G.O.,Dement, J.M.,Rao, V.A.,Eadsforth, T.C.,Hunter, W.N. (deposition date: 2011-01-13, release date: 2011-01-26, Last modification date: 2023-12-20) |
| Primary citation | Morgan, R.E.,Batot, G.O.,Dement, J.M.,Rao, V.A.,Eadsforth, T.C.,Hunter, W.N. Crystal Structures of Burkholderia Cenocepacia Dihydropteroate Synthase in the Apo-Form and Complexed with the Product 7,8-Dihydropteroate. Bmc Struct.Biol., 11:21-, 2011 Cited by PubMed Abstract: The enzyme dihydropteroate synthase (DHPS) participates in the de novo synthesis of folate cofactors by catalyzing the formation of 7,8-dihydropteroate from condensation of p-aminobenzoic acid with 6-hydroxymethyl-7,8-dihydropteroate pyrophosphate. DHPS is absent from humans, who acquire folates from diet, and has been validated as an antimicrobial therapeutic target by chemical and genetic means. The bacterium Burkholderia cenocepacia is an opportunistic pathogen and an infective agent of cystic fibrosis patients. The organism is highly resistant to antibiotics and there is a recognized need for the identification of new drugs against Burkholderia and related Gram-negative pathogens. Our characterization of the DHPS active site and interactions with the enzyme product are designed to underpin early stage drug discovery. PubMed: 21554707DOI: 10.1186/1472-6807-11-21 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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