Structural Basis for the ATP-dependent Configuration of Adenylation Active Site in Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase.

Chen, Yaozong; Sun, Yueru; Song, Haigang; Guo, Zhihong

Chen, Yaozong; Sun, Yueru; Song, Haigang; Guo, Zhihong.

Afiliação

Chen Y; From the Department of Chemistry and State Key Laboratory for Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Sun Y; From the Department of Chemistry and State Key Laboratory for Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Song H; From the Department of Chemistry and State Key Laboratory for Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Guo Z; From the Department of Chemistry and State Key Laboratory for Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China chguo@ust.hk.

J Biol Chem ; 290(39): 23971-83, 2015 Sep 25.

Article em En | MEDLINE | ID: mdl-26276389

Assuntos

Trifosfato de Adenosina/química; Bacillus subtilis/enzimologia; Modelos Moleculares; Succinato-CoA Ligases/química; Bacillus subtilis/genética; Catálise; Domínio Catalítico; Estrutura Secundária de Proteína; Especificidade por Substrato; Succinato-CoA Ligases/genética

Palavras-chave

ATP; adenylate forming enzyme; crystal structure; domain alteration; enzyme mechanism; open-closed conformational change; protein conformation; vitamin K

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Succinato-CoA Ligases / Bacillus subtilis / Modelos Moleculares / Trifosfato de Adenosina Tipo de estudo: Prognostic_studies Idioma: En Revista: J Biol Chem Ano de publicação: 2015 Tipo de documento: Article País de afiliação: China

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