5ll3

Structure of the Isoleucine 2-epimerase from Lactobacillus buchneri (PLP complex form)

spinqualitylabelsall models 5ll3, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ll3 is a 4 chain structure with sequence from Lentilactobacillus buchneri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ILE2E_LENBU Publication Abstract from PubMed The isoleucine 2-epimerase from Lactobacillus buchneri has been previously identified and characterized to catalyze the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine. In this study, crystal structures of both native and PLP-complex forms of this racemase are presented at 2.6 and 2.15 A resolution, respectively. Both structures show that the protein belongs to the fold-type I subgroup of PLP-dependent enzymes and is very close to aminobutyrate aminotransferases family, as it has been suspected because of their sequence homology. The extensive structural comparison with fold-type I enzymes with known amino acid racemization activities, including the alpha-amino-epsilon-caprolactam racemase from Achromobacter obae and the cystathionine beta-lyase from Escherichia coli, allows us to identify the active site residues responsible for its nonpolar amino acid recognition and reactivity specificity. Our observations also suggest that the racemization reaction by the fold-type I racemases may generally occur thanks to a revised two-base mechanism. Lastly, both structures reveal details on the conformational changes provoked by PLP binding that suggest an induced fit of the active site "entrance door", necessary to accommodate PLP and substrate molecules. Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri.,Awad R, Gans P, Reiser JB Biochimie. 2017 Mar 23. pii: S0300-9084(16)30277-2. doi:, 10.1016/j.biochi.2017.03.015. PMID:28344038 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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