Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox

Autor(es)

Feliciano, Patricia R. ; Rustiguel, Joane K. ; Soares, Ricardo O. S. ; Sampaio, Suely V. ; Cristina Nonato, M.

• Tipo de documento: Artigo Científico
• Fonte: Toxicon; v. 128, p. 50-59, MAR 15 2017.
• Citações Web of Science: 8

Resumo

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. (C) 2017 Elsevier Ltd. All rights reserved. (AU)

• Processo FAPESP: 15/24010-0 - Caracterização estrutural e biofísica de toxinas animais
• Beneficiário: Joane Kathelen Rustiguel Bonalumi
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 09/10454-3 - Estudos da correlação entre estrutura e função da enzima fumarato hidratase em Leishmania major
• Beneficiário: Patrícia Rosa Feliciano
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 13/14988-8 - Elucidação do mecanismo de ação da enzima fumarato hidratase de Leishmania major
• Beneficiário: Patrícia Rosa Feliciano
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado