한빛사논문
- 조회4,560
한국생명공학연구원(KRIBB)
Abstract
( quorum sensing | lactonase | metalloenzyme | crystal structure )
Myung Hee Kim *, Won-Chan Choi *, Hye Ok Kang *, Jong Suk Lee *, Beom Sik Kang 
, Kyung-Jin Kim 
, Zygmunt S. Derewenda 
, Tae-Kwang Oh ¶, Choong Hwan Lee *||, and Jung-Kee Lee *||
*Korea Research Institute of Bioscience and Biotechnology, Yusong, Daejon 305-600,Korea; School of Life Science and Biotechnology, Kyungpook National University, Daegu 702-701, Korea; Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, Korea; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908; and ¶21C Frontier Microbial Genomics and Applications Center, Korea Research Institute of Bioscience and Biotechnology, Yusong, Daejon 305-600, Korea
Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved October 13, 2005 (received for review June 15, 2005)
In many Gram-negative bacteria, including a number of pathogens such as Pseudomonas aeruginosa and Erwinia carotovora, virulence factor production and biofilm formation are linked to the quorum-sensing systems that use diffusible N-acyl-L-homoserine lactones (AHLs) as intercellular messenger molecules. A number of organisms also contain genes coding for lactonases that hydrolyze AHLs into inactive products, thereby blocking the quorum-sensing systems. Consequently, these enzymes attract intense interest for the development of antiinfection therapies. However, the catalytic mechanism of AHL-lactonase is poorly understood and subject to controversy. We here report a 2.0-Å resolution structure of the AHL-lactonase from Bacillus thuringiensis and a 1.7-Å crystal structure of its complex with L-homoserine lactone. Despite limited sequence similarity, the enzyme shows remarkable structural similarities to glyoxalase II and RNase Z proteins, members of the metallo-
-lactamase superfamily. We present experimental evidence that AHL-lactonase is a metalloenzyme containing two zinc ions involved in catalysis, and we propose a catalytic mechanism for bacterial metallo-AHL-lactonases.
Author contributions: M.H.K., T.-K.O., C.H.L., and J.-K.L. designed research; M.H.K., W.-C.C., H.O.K., J.S.L., B.S.K., and K.-J.K. performed research; M.H.K., W.-C.C., and J.S.L. contributed new reagents/analytic tools; M.H.K., W.-C.C., H.O.K., J.S.L., B.S.K., K.-J.K., Z.S.D., T.-K.O., C.H.L., and J.-K.L. analyzed data; and M.H.K., Z.S.D., C.H.L., and J.-K.L. wrote the paper.
Conflict of interest statement: No conflicts declared.
Freely available online through the PNAS open access option.
||To whom correspondence may be addressed.
논문정보
- Research article
- 2005년 11월 (BRIC 등록일 )
- 국내(교신)+국외 연구진
- 생명과학 > 미생물학
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