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Crystal structure of the EnvZ periplasmic domain with CHAPS.
Hwang, Eunha; Cheong, Hae-Kap; Kim, Sang-Yoon; Kwon, Ohsuk; Blain, Katherine Y; Choe, Senyon; Yeo, Kwon Joo; Jung, Yong Woo; Jeon, Young Ho; Cheong, Chaejoon.
Afiliação
  • Hwang E; Division of Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Chungbuk, Korea.
  • Cheong HK; Division of Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Chungbuk, Korea.
  • Kim SY; Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, Korea.
  • Kwon O; Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, Korea.
  • Blain KY; Qualcomm Institute, University of California San Diego, San Diego, CA, USA.
  • Choe S; Qualcomm Institute, University of California San Diego, San Diego, CA, USA.
  • Yeo KJ; College of Pharmacy, Korea University, Sejong, Korea.
  • Jung YW; College of Pharmacy, Korea University, Sejong, Korea.
  • Jeon YH; College of Pharmacy, Korea University, Sejong, Korea.
  • Cheong C; Division of Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Chungbuk, Korea.
FEBS Lett ; 591(10): 1419-1428, 2017 05.
Article em En | MEDLINE | ID: mdl-28423182
Bacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and ß-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with ß-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas da Membrana Bacteriana Externa / Ácidos Cólicos / Colatos / Proteínas de Escherichia coli / Detergentes / Escherichia coli / Complexos Multienzimáticos Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas da Membrana Bacteriana Externa / Ácidos Cólicos / Colatos / Proteínas de Escherichia coli / Detergentes / Escherichia coli / Complexos Multienzimáticos Idioma: En Ano de publicação: 2017 Tipo de documento: Article