4cw5

Crystal structure of the enoyl reductase domain of DfnA from Bacillus amyloliquefaciens

spinqualitylabelsall models 4cw5, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cw5 is a 2 chain structure with sequence from Bacillus velezensis FZB42. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A7Z6E3_BACVZ] Publication Abstract from PubMed Fungal fatty acid synthase (fFAS) is a key paradigm for the evolution of complex multienzymes. Its 48 functional domains are embedded in a matrix of scaffolding elements, which comprises almost 50% of the total sequence and determines the emergent multienzymes properties of fFAS. Catalytic domains of fFAS are derived from monofunctional bacterial enzymes, but the evolutionary origin of the scaffolding elements remains enigmatic. Here, we identify two bacterial protein families of noncanonical fatty acid biosynthesis starter enzymes and trans-acting polyketide enoyl reductases (ERs) as potential ancestors of scaffolding regions in fFAS. The architectures of both protein families are revealed by representative crystal structures of the starter enzyme FabY and DfnA-ER. In both families, a striking structural conservation of insertions to scaffolding elements in fFAS is observed, despite marginal sequence identity. The combined phylogenetic and structural data provide insights into the evolutionary origins of the complex multienzyme architecture of fFAS. Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase.,Bukhari HS, Jakob RP, Maier T Structure. 2014 Dec 2;22(12):1775-85. doi: 10.1016/j.str.2014.09.016. Epub 2014, Nov 13. PMID:25456814 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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