Your browser doesn't support javascript.
loading
The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.
Kobayashi, Kan; Katz, Assaf; Rajkovic, Andrei; Ishii, Ryohei; Branson, Owen E; Freitas, Michael A; Ishitani, Ryuichiro; Ibba, Michael; Nureki, Osamu.
Afiliação
  • Kobayashi K; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan Global Research Cluster, RIKEN, 2-1, Hirosawa, Wako, Saitama, 351-0198, Japan.
  • Katz A; Department of Microbiology, Ohio State University, Columbus, OH 43210, USA.
  • Rajkovic A; Molecular, Cell, and Developmental Biology Program, Ohio State University, Columbus, OH 43210, USA.
  • Ishii R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan Global Research Cluster, RIKEN, 2-1, Hirosawa, Wako, Saitama, 351-0198, Japan.
  • Branson OE; Department of Biochemistry, Ohio State University, Columbus, OH 43210, USA.
  • Freitas MA; Comprehensive Cancer Center, Ohio State University, Columbus, OH 43210, USA Department of Molecular Virology, Immunology and Medical Genetics, Ohio State University, Columbus, OH 43210, USA.
  • Ishitani R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan Global Research Cluster, RIKEN, 2-1, Hirosawa, Wako, Saitama, 351-0198, Japan.
  • Ibba M; Department of Microbiology, Ohio State University, Columbus, OH 43210, USA Ohio State Biochemistry Program, Center for RNA Biology, Ohio State University, Columbus, OH 43210, USA.
  • Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan Global Research Cluster, RIKEN, 2-1, Hirosawa, Wako, Saitama, 351-0198, Japan nureki@bs.s.u-tokyo.ac.jp.
Nucleic Acids Res ; 42(19): 12295-305, 2014 Oct 29.
Article em En | MEDLINE | ID: mdl-25274739
Assuntos
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fatores de Alongamento de Peptídeos / Proteínas de Escherichia coli / Oxigenases de Função Mista / Metais Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2014 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fatores de Alongamento de Peptídeos / Proteínas de Escherichia coli / Oxigenases de Função Mista / Metais Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2014 Tipo de documento: Article