Bulletin of the Korean Chemical Society

  • 제31권9호
  • /
  • Pages.2627-2632
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  • 2010
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Biochemical and Structural Analysis of Hormone-sensitive Lipase Homolog EstE7: Insight into the Stabilized Dimerization of HSL-Homolog Proteins

  • Nam, Ki-Hyun (Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University) ;
  • Park, Sung-Ha (Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University) ;
  • Lee, Won-Ho (Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University) ;
  • Hwang, Kwang-Yeon (Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University)
  • 투고 : 2010.03.25
  • 심사 : 2010.06.07
  • 발행 : 2010.09.20
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초록

Hormone sensitive lipase (HSL) plays a major role in energy homeostasis and lipid metabolism. Several crystal structures of HSL-homolog proteins have been identified, which has led to a better understanding of its molecular function. HSL-homolog proteins exit as both monomer and dimer, but the biochemical and structural basis for such oligomeric states has not been successfully elucidated. Therefore, we determined the crystal structure of HSL-homolog protein EstE7 from a metagenome library at $2.2\;{\AA}$ resolution and characterized the oligomeric states of EstE7 both structurally and biochemically. EstE7 protein prefers the dimeric state in solution, which is supported by its higher enzymatic activity in the dimeric state. In the crystal form, EstE7 protein shows two-types of dimeric interface. Specifically, dimerization via the external ${beta}8$-strand occurred through tight association between two pseudosymmetric folds via salt bridges, hydrogen bonds and van der Waals interactions. This dimer formation was similar to that of other HSL-homolog protein structures such as AFEST, BEFA, and EstE1. We anticipate that our results will provide insight into the oligomeric state of HSL-homolog proteins.

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피인용 문헌

  1. Triglycine-Based Approach for Identifying the Substrate Recognition Site of an Enzyme vol.9, pp.9, 2010, https://doi.org/10.3390/cryst9090444