4E0V

Structure of L-amino acid oxidase from the B. jararacussu venom

Summary for 4E0V

• Entry DOI: 10.2210/pdb4e0v/pdb
• Descriptor: L-amino-acid oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: l-amino acid oxidase, fad-binding mode, oxidoreductase
• Biological source: Bothrops jararacussu (Jararacussu)
• Cellular location: Secreted (By similarity): Q6TGQ9
• Total number of polymer chains: 2
• Total formula weight: 114288.01

Authors

Ullah, A.,Souza, T.A.C.B.,Betzel, C.,Murakami, M.T.,Arni, R.K. (deposition date: 2012-03-05, release date: 2012-04-25, Last modification date: 2024-11-27)

Primary citation

Ullah, A.,Souza, T.A.,Abrego, J.R.,Betzel, C.,Murakami, M.T.,Arni, R.K.
Structural insights into selectivity and cofactor binding in snake venom L-amino acid oxidases.
Biochem.Biophys.Res.Commun., 421:124-128, 2012

PubMed Abstract: L-Amino acid oxidases (LAAOs) are flavoenzymes that catalytically deaminate L-amino acids to corresponding α-keto acids with the concomitant production of ammonia (NH(3)) and hydrogen peroxide (H(2)O(2)). Particularly, snake venom LAAOs have been attracted much attention due to their diverse clinical and biological effects, interfering on human coagulation factors and being cytotoxic against some pathogenic bacteria and Leishmania ssp. In this work, a new LAAO from Bothrops jararacussu venom (BjsuLAAO) was purified, functionally characterized and its structure determined by X-ray crystallography at 3.1 Å resolution. BjsuLAAO showed high catalytic specificity for aromatic and aliphatic large side-chain amino acids. Comparative structural analysis with prokaryotic LAAOs, which exhibit low specificity, indicates the importance of the active-site volume in modulating enzyme selectivity. Surprisingly, the flavin adenine dinucleotide (FAD) cofactor was found in a different orientation canonically described for both prokaryotic and eukaryotic LAAOs. In this new conformational state, the adenosyl group is flipped towards the 62-71 loop, being stabilized by several hydrogen-bond interactions, which is equally stable to the classical binding mode.

PubMed: 22490662
DOI: 10.1016/j.bbrc.2012.03.129

Experimental method

X-RAY DIFFRACTION (3.1 Å)