来自枯草芽孢杆菌的L-氨基酸连接酶RizA的结构。
Structure of RizA, an L-amino-acid ligase from Bacillus subtilis.
作者信息
Kagawa Wataru, Arai Toshinobu, Ishikura Shun, Kino Kuniki, Kurumizaka Hitoshi
机构信息
Department of Interdisciplinary Science and Engineering, Program in Chemistry and Life Science, School of Science and Engineering, Meisei University, 2-1-1 Hodokubo, Hino-shi, Tokyo 191-8506, Japan.
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan.
出版信息
Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi: 10.1107/S2053230X15012698. Epub 2015 Aug 25.
Abstract
RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 Å resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies.
摘要
RizA是一种来自枯草芽孢杆菌的L-氨基酸连接酶，参与寡肽抗生素根霉素的生物合成。RizA的无底物形式已被结晶，并以2.8 Å的分辨率解析了其结构。氨基酸结合位点似乎能够容纳多个氨基酸，这与之前的生化研究结果一致。
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