Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop
Year: 2005
Type: article
Abstract: Monomeric sarcosine oxidase (MSOX) is a flavoprotein that catalyzes the oxidation of sarcosine to generate formaldehyde, glycine, and hydrogen peroxide, and is utilized in quantification of creatinine in serum. Crystal structure of MSOX from Bacillus sp. NS-129 (without ligand) has been determined at 1.86 Å Unlike the published structures of MSOX from Bacillus sp. B-0618 (without or with carboxylate-containing ligand), the two molecules in the asymmetric unit adopt distinct conformations at the active site loop (Gly56 to Glu60) with a maximal root-mean-square (RMS) displacement of 3.3 Å for Cα atom of Arg59. The multiple conformations seen at the active-site loop suggest that high flexibility of the loop would be important for the activity of MSOX. (Communicated by Masanori OTSUKA, M.J.A.)
DOI: 10.2183/pjab.81.220
Authors: Koji NAGATA, Hiroshi SASAKI, Ming HUA, Masahiko OKAI, Keiko KUBOTA, Masayuki KAMO, Kosuke ITO, Toshio ICHIKAWA, Yasuji KOYAMA, Masaru TANOKURA
Institutions: The University of Tokyo, Kikkoman (Japan)
Language: English
Subfield: Structural Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1967525201