NDLI: The structure of a native l-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions

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The structure of a native l-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions

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Molecular BioSystems Vol -6

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The structure of a native l-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions

Content Provider	Royal Society of Chemistry (RSC)
Author	Murakami, Mario Betzel, Christian Arni, Raghuvir Perband, Markus Georgieva, Dessislava
Copyright Year	2011
Abstract	The crystal structure of the major component of the Vipera ammodytes ammodytes venomic, a flavotoxin, member of the L-amino acid oxidase (LAAO) family, has been determined and refined at 2.6 Å resolution. The asymmetric unit consists of four molecules, each bound to oxidized FAD, representing a dimer of dimers. The binding of four Zn2+ ions stabilizes the enzymatically active quaternary structure and is considered important for the biological activity of LAAO and other flavoproteins. Each monomer consists of three domains with a cofactor bound between the FAD and substrate binding domains, and a solvent exposed glycosylation site which is considered crucial for the toxicity. Comparison of LAAO structures in the absence and presence of a substrate indicates conformational changes in the dynamic active site. The active site H-bond network involving the triad Lys326–Water–N5 of FAD is formed only upon substrate binding, and results in the increased mobility of the isoalloxazine system. Details of the catalytic transformation of amino acid substrates are discussed.
Starting Page	379
Ending Page	384
Page Count	6
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	2
Journal	Molecular BioSystems
DOI	10.1039/c0mb00101e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	LAAO Active site Oxidase Cofactor (biochemistry) Glycosylation Protein dimer Biomolecular structure Flavin group Catalytic triad Vipera ammodytes Carboxylic acid Flavin adenine dinucleotide Protein subunit Solvent
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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