2yr6 | pdb_00002yr6

Crystal structure of L-phenylalanine oxidase from Psuedomonas sp.P501

spinqualitylabelsall models 2yr6, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yr6 is a 2 chain structure with sequence from Pseudomonas sp. P-501. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: BE2, FAD, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAO_PSESP Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The mature form of l-phenylalanine oxidase (PAOpt) from Pseudomonas sp. P-501 was generated and activated by the proteolytic cleavage of a noncatalytic proenzyme (proPAO). The crystal structures of proPAO, PAOpt, and the PAOpt-o-amino benzoate (AB) complex were determined at 1.7, 1.25, and 1.35A resolutions, respectively. The structure of proPAO suggests that the prosequence peptide of proPAO occupies the funnel (pathway) of the substrate amino acid from the outside of the protein to the interior flavin ring, whereas the funnel is closed with the hydrophobic residues at its vestibule in both PAOpt and the PAOpt-AB complex. All three structures have an oxygen channel that is open to the surface of the protein from the flavin ring. These results suggest that structural changes were induced by proteolysis; that is, the proteolysis of proPAO removes the prosequence and closes the funnel to keep the active site hydrophobic but keeps the oxygen channel open. The possibility that an interaction of the hydrophobic side chain of substrate with the residues of the vestibule region may open the funnel as a putative amino acid channel is discussed. Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501.,Ida K, Kurabayashi M, Suguro M, Hiruma Y, Hikima T, Yamomoto M, Suzuki H J Biol Chem. 2008 Jun 13;283(24):16584-90. doi: 10.1074/jbc.M800366200. Epub 2008, Apr 16. PMID:18417467 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA