5TS5

Crystal structure of L-amino acid oxidase from Bothrops atrox

Summary for 5TS5

• Entry DOI: 10.2210/pdb5ts5/pdb
• Descriptor: Amine oxidase, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, FLAVIN-ADENINE DINUCLEOTIDE, ... (7 entities in total)
• Functional Keywords: snake venom, oxidoreductase
• Biological source: Bothrops atrox (Barba amarilla)
• Total number of polymer chains: 4
• Total formula weight: 225419.58

Authors

Feliciano, P.R.,Nonato, M.C. (deposition date: 2016-10-27, release date: 2017-04-26, Last modification date: 2024-10-30)

Primary citation

Feliciano, P.R.,Rustiguel, J.K.,Soares, R.O.,Sampaio, S.V.,Cristina Nonato, M.
Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.
Toxicon, 128:50-59, 2017

PubMed Abstract: L-amino acid oxidases (LAAOs) are dimeric flavoproteins that catalyze the deamination of L-amino acid to α-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.

PubMed: 28137621
DOI: 10.1016/j.toxicon.2017.01.017

Experimental method

X-RAY DIFFRACTION (2.3 Å)