3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound.

Brignole, Edward J; Tsai, Kuang-Lei; Chittuluru, Johnathan; Li, Haoran; Aye, Yimon; Penczek, Pawel A; Stubbe, JoAnne; Drennan, Catherine L; Asturias, Francisco

Brignole, Edward J; Tsai, Kuang-Lei; Chittuluru, Johnathan; Li, Haoran; Aye, Yimon; Penczek, Pawel A; Stubbe, JoAnne; Drennan, Catherine L; Asturias, Francisco.

Afiliação

Brignole EJ; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, United States.
Tsai KL; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Chittuluru J; Department of Integrative Computational and Structural Biology, The Scripps Research Institute, La Jolla, United States.
Li H; Department of Integrative Computational and Structural Biology, The Scripps Research Institute, La Jolla, United States.
Aye Y; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.
Penczek PA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.
Stubbe J; Department of Biochemistry and Molecular Biology, The University of Texas-Houston Medical School, Houston, United States.
Drennan CL; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Asturias F; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.

Elife ; 72018 02 20.

Article em En | MEDLINE | ID: mdl-29460780

Assuntos

Multimerização Proteica; Ribonucleotídeo Redutases/química; Trifosfato de Adenosina/química; Trifosfato de Adenosina/metabolismo; Regulação Alostérica; Microscopia Crioeletrônica; Cistina Difosfato/química; Cistina Difosfato/metabolismo; Humanos; Modelos Moleculares; Ligação Proteica; Conformação Proteica; Ribonucleotídeo Redutases/metabolismo

Palavras-chave

E. coli; allosteric regulation; biochemistry; biophysics; chemical biology; chemotherapeutic target; human; nucleic acid metabolism; protein structure; radical mechanism; single-particle electron microscopy; structural biology

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Texto completo: 1 Coleções: 01-internacional Temas: Geral Base de dados: MEDLINE Assunto principal: Ribonucleotídeo Redutases / Multimerização Proteica Limite: Humans Idioma: En Revista: Elife Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Estados Unidos

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