The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis.

The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Research Abstract Details 

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The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Abstract Text:

Ella Czarina Magat Juan,Md Mominul Hoque,Md Tofazzal Hossain,Tamotsu Yamamoto,Shigeyuki Imamura,Kaoru Suzuki,Takeshi Sekiguchi,Akio ,Ella Czarina Magat Juan,Md Mominul Hoque,Md Tofazzal Hossain,Tamotsu Yamamoto,Shigeyuki Imamura,Kaoru Suzuki,Takeshi Sekiguchi,Akio ,

The crystal structures of pyruvate oxidase from Aerococcus viridans (AvPOX) complexed with flavin adenine dinucleotide (FAD), with FAD and thiamine diphosphate (ThDP) and with FAD and the 2-acetyl-ThDP intermediate (AcThDP) have been determined at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric AvPOX enzyme consists of three domains, as observed in other ThDP-dependent enzymes. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while ThDP is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Of particular interest is the role of Lys478, the side chain of which may be bent or extended depending on the stage of catalysis. The structures also provide insight into the routes for electron transfer to FAD and the involvement of active-site residues in the catalysis of pyruvate to its products.

The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Publishing Authors By Initials

EC Juan,MM Hoque,MT Hossain,T Yamamoto,S Imamura,K Suzuki,T Sekiguchi,A ,EC Juan,MM Hoque,MT Hossain,T Yamamoto,S Imamura,K Suzuki,T Sekiguchi,A ,

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The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Acta crystallographica. Section F, Structural biol

VOLUME: 63

Page Numbers: 900-7

Journal Abbreviation: Acta Crystallogr. Sect. F Stru

ISSN: 1744-3091

DAY: 20

MONTH: 10

YEAR: 2007

The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Information

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LANGUAGE: eng

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Grant and Affiliation Information for The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis.

AFFILIATION: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.

Country: England

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MEDLINETA: Acta Crystallogr Sect F Struct

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