Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6

Nishi, Kosuke; Lee, Hyun-Ju; Park, Suk-Youl; Bae, Soo Jang; Lee, Shee Eun; Adams, Paul D.; Rhee, Joon Haeng; Kim, Jeong-Sun

doi:10.1016/j.febslet.2010.02.052

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Volume 584, Issue 6 , Pages 1097-1102, 19 March 2010

Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6

Edited by Hans Eklund

Kosuke Nishi
- Department of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea
Hyun-Ju Lee
- Department of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea
Suk-Youl Park
- Department of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea
Soo Jang Bae
- Clinical Vaccine R&D Center, Research Institute of Vibrio Infections and Department of Microbiology, Chonnam National University Medical School, Gwangju 501-746, Republic of Korea
Shee Eun Lee
- Department of Dental Pharmacology, College of Dentistry, Chonnam National University, Gwangju 500-757, Republic of Korea
Paul D. Adams
- Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Joon Haeng Rhee
- Clinical Vaccine R&D Center, Research Institute of Vibrio Infections and Department of Microbiology, Chonnam National University Medical School, Gwangju 501-746, Republic of Korea
Jeong-Sun Kim
- Department of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea
- Corresponding author. Address: Department of Chemistry, Chonnam National University, 300, Yongbong-dong, Buk-gu, Gwangju 500-757, Republic of Korea. Fax: +82 62 530 3389.

Received 14 December 2009; received in revised form 17 February 2010; accepted 17 February 2010. published online 22 February 2010.

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 α-helices and two β-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.