TAILIEUCHUNG - Báo cáo khoa học: Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris

Glutaminase from Micrococcus luteusK-3 [Micrococcusglutaminase (Mglu); 456 amino acid residues (aa); 48 kDa] is a salt-tolerant enzyme. Our previous study determined the structure of its major 42-kDa fragment. Here, using new crystallization conditions, we determined the structures of the intact enzyme in the presence and absence of its product l-glutamate and its activator Tris, which activates the enzyme by sixfold. | Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris Kazuaki Yoshimune1 Yasuo Shirakihara2 Mamoru Wakayama3 and Isao Yumoto1 1 Research Institute of Genome-based Biofactory National institute of Advanced Industrial science and Technology AIST Sapporo Hokkaido Japan 2 StructuralBiology Center National institute of Genetics Mishima Shizuoka Japan 3 Department of Biotechnology Faculty of Life Science Ritsumeikan University Kusatsu Shiga Japan Keywords crystal structure L-glutamate Micrococcus luteus K-3 salt-tolerant glutaminase Tris Correspondence K. Yoshimune Research Institute of Genome-based Biofactory NationalInstitute of Advanced IndustrialScience and Technology AIST Tsukisamu-Higashi Toyohira-ku Sapporo Hokkaido 062-8517 Japan Fax 81 11 857 8980 Tel 81 11 857 8444 E-mail Note Coordinates and structure factors have been deposited in the Protein Data Bank under accession codes 3ih8 N 3ih9 T 3iha G and 3ihb TG Received 5 September 2009 revised 1 November 2009 accepted 26 November 2009 doi Glutaminase from Micrococcus luteus K-3 Micrococcus glutaminase Mglu 456 amino acid residues aa 48 kDa is a salt-tolerant enzyme. Our previous study determined the structure of its major 42-kDa fragment. Here using new crystallization conditions we determined the structures of the intact enzyme in the presence and absence of its product L-glutamate and its activator Tris which activates the enzyme by sixfold. With the exception of a lid part 26-29 aa and a few other short stretches the structures were all very similar over the entire polypeptide chain. However the presence of the ligands significantly reduced the length of the disordered regions 41 aa in the unliganded structure N 21 aa for L-glutamate G 8 aa for Tris T and 6 aa for both L-glutamate and Tris TG . L-Glutamate was identified in both the G and TG structures .

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