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Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6 SCIE SCOPUS

Title
Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6
Authors
Nishi, KLee, HJPark, SYBae, SJLee, SEAdams, PDRhee, JHKim, JS
Date Issued
2010-03
Publisher
Elsevier BV
Abstract
HlyU is a transcription factor of the ArsR/SmtB family and activates the expression of the pathogenic Vibrio vulnificus RTX toxin. In contrast to the other metal-responding ArsR/SmtB proteins, HlyU does not sense metal ions. To provide its structural information, we elucidated the crystal structure of HlyU from V. vulnificus CMCP6 (HlyU_Vv). The monomeric HlyU_Vv architecture of five alpha-helices and two beta-strands, some of which constitute a typical DNA-binding winged helix-turn-helix (wHTH) motif, is very similar to that of other transcription regulators. Nonetheless, the homo-dimeric HlyU_Vv structure shows several different, three-dimensional features in the spatial position and the detailed dimeric interaction, which were not observed in the modeling study based on the same protein family and sequence similarity. Structured summary: MINT-7710072, MINT-7710086: HlyU_Vv ( uniprotkb: Q8DES3) and HlyU_Vv (uniprotkb: Q8DES3) bind (MI: 0407) by X-ray crystallography (MI: 0114) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
URI
https://oasis.postech.ac.kr/handle/2014.oak/109130
DOI
10.1016/j.febslet.2010.02.052
ISSN
0014-5793
Article Type
Article
Citation
FEBS Letters, vol. 584, no. 6, page. 1097 - 1102, 2010-03
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