6k1r

Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa in complex with NAD+ and ketopantoate

spinqualitylabelsall models 6k1r, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6k1r is a 3 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: GOL, KPL, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PANE_PSEAE Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. Publication Abstract from PubMed Ketopantoate reductases (KPRs) catalyse NADPH-dependent reduction of ketopantoate to pantoate, the rate-limiting step of pantothenate biosynthetic pathway. In our recent study, we showed KPRs are under dynamic evolutionary selection and highlighted the possible role of ordered substrate binding kinetics for cofactor selection. To further delineate this at molecular level, here, we perform X-ray crystallographic and biophysical analyses of KPR in presence of non-canonical cofactor NAD(+). In our structure, NAD(+) was found to be highly dynamic in catalytic pocket of KPR, which could attain stable conformation only in presence of ketopantoate. Further, isothermal calorimetric (ITC) titrations showed that affinity of KPR for ketopantoate is higher in presence of NADP(+) than in presence of NAD(+) and lowest in absence of redox cofactors. In sum, our results clearly depict two modes of redox cofactor selections in KPRs, firstly by specific salt bridge interactions with unique phosphate moiety of NADP(+) and secondly via ordered sequential heterotrophic cooperative binding of substrate ketopantoate. Crystallographic and biophysical analyses of Pseudomonas aeruginosa ketopantoate reductase: Implications of ligand induced conformational changes in cofactor recognition.,Choudhury A, Khanppnavar B, Datta S Biochimie. 2021 Oct 30. pii: S0300-9084(21)00252-2. doi:, 10.1016/j.biochi.2021.10.015. PMID:34757166 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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