5a88

Crystal structure of the riboflavin kinase module of FAD synthetase from Corynebacterium ammoniagenes in complex with ADP

spinqualitylabelsall models 5a88, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a88 is a 4 chain structure with sequence from Corynebacterium ammoniagenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.08Å Ligands: ADP, CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIBF_CORAM Publication Abstract from PubMed Riboflavin kinases (RFKs) catalyse the phosphorylation of riboflavin to produce FMN. In most bacteria this activity is catalysed by the C-terminal module of a bifunctional enzyme, FAD synthetase (FADS), which also catalyses the transformation of FMN into FAD through its N-terminal FMN adenylyltransferase (FMNAT) module. The RFK module of FADS is a homologue of eukaryotic monofunctional RFKs, while the FMNAT module lacks homologyto eukaryotic enzymes involved in FAD production. Previously, the crystal structure of Corynebacterium ammoniagenes FADS (CaFADS) was determined in its apo form. This structure predicted a dimer-of-trimers organization with the catalytic sites of two modules of neighbouring protomers approaching each other, leading to a hypothesis about the possibility of FMN channelling in the oligomeric protein. Here, two crystal structures of the individually expressed RFK module of CaFADS in complex with the products of the reaction, FMN and ADP, are presented. Structures are complemented with computational simulations, binding studies and kinetic characterization. Binding of ligands triggers dramatic structural changes in the RFK module, which affect large portions of the protein. Substrate inhibition and molecular-dynamics simulations allowed the conformational changes that take place along the RFK catalytic cycle to be established. The influence of these conformational changes in the FMNAT module is also discussed in the context of the full-length CaFADS protomer and the quaternary organization. Structural insights into the synthesis of FMN in prokaryotic organisms.,Herguedas B, Lans I, Sebastian M, Hermoso JA, Martinez-Julvez M, Medina M Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2526-42. doi:, 10.1107/S1399004715019641. Epub 2015 Nov 27. PMID:26627660 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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