2E1M

Crystal Structure of L-Glutamate Oxidase from Streptomyces sp. X-119-6

Summary for 2E1M

• Entry DOI: 10.2210/pdb2e1m/pdb
• Descriptor: L-glutamate oxidase, PHOSPHATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: l-amino acid oxidase, l-glutamate oxidase, fad, l-gox, flavoprotein, oxidoreductase
• Biological source: Streptomyces sp.; More
• Total number of polymer chains: 3
• Total formula weight: 77501.60

Authors

Sasaki, C.,Kashima, A.,Sakaguchi, C.,Mizuno, H.,Arima, J.,Kusakabe, H.,Tamura, T.,Sugio, S.,Inagaki, K. (deposition date: 2006-10-26, release date: 2007-11-13, Last modification date: 2023-10-25)

Primary citation

Arima, J.,Sasaki, C.,Sakaguchi, C.,Mizuno, H.,Tamura, T.,Kashima, A.,Kusakabe, H.,Sugio, S.,Inagaki, K.
Structural characterization of l-glutamate oxidase from Streptomyces sp. X-119-6
Febs J., 276:4318-4327, 2009

PubMed Abstract: L-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6, which catalyzes the oxidative deamination of L-glutamate, has attracted increasing attention as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry. The precursor of LGOX, which has a homodimeric structure, is less active than the mature enzyme with an alpha(2)beta(2)V(2) structure; enzymatic proteolysis of the precursor forms the stable mature enzyme. We solved the crystal structure of mature LGOX using molecular replacement with a structurally homologous model of L-amino acid oxidase (LAAO) from snake venom: LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site. Comparison of the LGOX structure with that of LAAO revealed that LGOX has three regions that are absent from the LAAO structure, one of which is involved in the formation of the entrance. Furthermore, the arrangement of the residues composing the active site differs between LGOX and LAAO, and the active site of LGOX is narrower than that of LAAO. Results of the comparative analyses described herein raise the possibility that such a unique structure of LGOX is associated with its substrate specificity.

PubMed: 19531050
DOI: 10.1111/j.1742-4658.2009.07103.x

Experimental method

X-RAY DIFFRACTION (2.8 Å)