5ts5

Crystal structure of L-amino acid oxidase from Bothrops atrox

spinqualitylabelsall models 5ts5, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ts5 is a 4 chain structure with sequence from Bothrops atrox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, FUC, GOL, NAG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed L-amino acid oxidases (LAAOs) are dimeric flavoproteins that catalyze the deamination of L-amino acid to alpha-keto acid, producing ammonia and hydrogen peroxide. In this study, we report the crystal structure and molecular dynamics simulations of LAAO from the venom of Bothrops atrox (BatroxLAAO). BatroxLAAO presents several biological and pharmacological properties with promising biomedical applications. BatroxLAAO structure contains the highly conserved structural pattern of LAAOs comprising a FAD-binding domain, substrate-binding domain and helical domain, and a dimeric arrangement that can be stabilized by zinc. Also, molecular dynamics results show an asymmetric behavior, and a direct communication between FAD- and substrate-binding domains of counterpart subunits. These findings shed light on the structural role of dimerization to catalytic mechanism of SV-LAAOs. Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.,Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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