4fxu

Crystallographic structure of trimeric riboflavin synthase from Brucella abortus

spinqualitylabelsall models 4fxu, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fxu is a 3 chain structure with sequence from "bacillus_of_abortion"_bang_1897 "bacillus of abortion" bang 1897. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4e0f, 1i8d, 1kzl Gene: RIBE ("Bacillus of abortion" Bang 1897) Activity: Riboflavin synthase, with EC number 2.5.1.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Riboflavin synthase (RS) catalyzes the last step of riboflavin biosynthesis in microorganisms and plants, which corresponds to the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine to yield one molecule of riboflavin and one molecule of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. Owing to the absence of this enzyme in animals and the fact that most pathogenic bacteria show a strict dependence on riboflavin biosynthesis, RS has been proposed as a potential target for antimicrobial drug development. Eubacterial, fungal and plant RSs assemble as homotrimers lacking C3 symmetry. Each monomer can bind two substrate molecules, yet there is only one active site for the whole enzyme, which is located at the interface between two neighbouring chains. This work reports the crystallographic structure of RS from the pathogenic bacterium Brucella abortus (the aetiological agent of the disease brucellosis) in its apo form, in complex with riboflavin and in complex with two different product analogues, being the first time that the structure of an intact RS trimer with bound ligands has been solved. These crystal models support the hypothesis of enhanced flexibility in the particle and also highlight the role of the ligands in assembling the unique active site. Kinetic and binding studies were also performed to complement these findings. The structural and biochemical information generated may be useful for the rational design of novel RS inhibitors with antimicrobial activity. Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility.,Serer MI, Bonomi HR, Guimaraes BG, Rossi RC, Goldbaum FA, Klinke S Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1419-34. doi:, 10.1107/S1399004714005161. Epub 2014 Apr 30. PMID:24816110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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