Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M. Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox. Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621 doi:http://dx.doi.org/10.1016/j.toxicon.2017.01.017
