Trading in catalytic power for sensing.

Hei, Zhoufei; Wang, Jing; Fang, Pengfei

Hei, Zhoufei; Wang, Jing; Fang, Pengfei.

Afiliação

Hei Z; School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China.
Wang J; School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China; State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China.
Fang P; School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China; State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China. Electronic address: fangpengfei@sioc.ac.cn.

Structure ; 32(6): 647-649, 2024 Jun 06.

Article em En | MEDLINE | ID: mdl-38848680

ABSTRACT

ABSTRACT

In this issue of Structure, Yin et al.1 present the CryoEM structure of the HisRS-like domain of human GCN2 and demonstrate that it is a pseudoenzyme, which binds uncharged tRNA in a different manner than HisRS and does not bind histidine and ATP.

Assuntos

Trifosfato de Adenosina; Humanos; Trifosfato de Adenosina/metabolismo; Trifosfato de Adenosina/química; Microscopia Crioeletrônica; RNA de Transferência/metabolismo; RNA de Transferência/química; Proteínas Serina-Treonina Quinases/metabolismo; Proteínas Serina-Treonina Quinases/química; Catálise; Modelos Moleculares; Histidina/química; Histidina/metabolismo

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Trifosfato de Adenosina Limite: Humans Idioma: En Revista: Structure Ano de publicação: 2024 Tipo de documento: Article

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