Crystal Structure of the Regulatory Domain of AphB from Vibrio vulnificus , a Virulence Gene Regulator
The transcriptional activator AphB has been implicated in acid resistance and pathogenesis in the food borne pathogens and . To date, the full-length AphB crystal structure of has been determined and characterized by a tetrameric assembly of AphB consisting of a DNA binding domain and a regulatory d...
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Published in: | Molecules and cells Vol. 40; no. 4; pp. 299 - 306 |
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Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Korean Society for Molecular and Cellular Biology
01-04-2017
한국분자세포생물학회 |
Subjects: | |
Online Access: | Get full text |
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Summary: | The transcriptional activator AphB has been implicated in acid resistance and pathogenesis in the food borne pathogens
and
. To date, the full-length AphB crystal structure of
has been determined and characterized by a tetrameric assembly of AphB consisting of a DNA binding domain and a regulatory domain (RD). Although acidic pH and low oxygen tension might be involved in the activation of AphB, it remains unknown which ligand or stimulus activates AphB at the molecular level. In this study, we determine the crystal structure of the AphB RD from
under aerobic conditions without modification at the conserved cysteine residue of the RD, even in the presence of the oxidizing agent cumene hydroperoxide. A cysteine to serine amino acid residue mutant RD protein further confirmed that the cysteine residue is not involved in sensing oxidative stress in vitro. Interestingly, an unidentified small molecule was observed in the inter-subdomain cavity in the RD when the crystal was incubated with cumene hydroperoxide molecules, suggesting a new ligand-binding site. In addition, we confirmed the role of AphB in acid tolerance by observing an
-dependent increase in
transcript level when
was exposed to acidic pH. Our study contributes to the understanding of the AphB molecular mechanism in the process of recognizing the host environment. |
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Bibliography: | These authors contributed equally to this work |
ISSN: | 1016-8478 0219-1032 |
DOI: | 10.14348/molcells.2017.0015 |