[논문]Non-Cryogenic Structure and Dynamics of HIV-1 Integrase Catalytic Core Domain by X-ray Free-Electron Lasers

Park, Jae-Hyun; Yun, Ji-Hye; Shi, Yingchen; Han, Jeongmin; Li, Xuanxuan; Jin, Zeyu; Kim, Taehee; Park, Jaehyun; Park, Sehan; Liu, Haiguang; Lee, Weontae

doi:10.3390/ijms20081943

Non-Cryogenic Structure and Dynamics of HIV-1 Integrase Catalytic Core Domain by X-ray Free-Electron Lasers 원문보기

International journal of molecular sciences, v.20 no.8, 2019년, pp.1943 -

Park, Jae-Hyun (Structural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea) , Yun, Ji-Hye (jaehyun234@yonsei.ac.kr (J.-H.P.)) , Shi, Yingchen (jihye2@spin.yonsei.ac.kr (J.-H.Y.)) , Han, Jeongmin (jmhan@spin.yonsei.ac.kr (J.H.)) , Li, Xuanxuan (zyjin@spin.yonsei.ac.kr (Z.J.)) , Jin, Zeyu (thkim@spin.yonsei.ac.kr (T.K.)) , Kim, Taehee (Structural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea) , Park, Jaehyun (jaehyun234@yonsei.ac.kr (J.-H.P.)) , Park, Sehan (jihye2@spin.yonsei.ac.kr (J.-H.Y.)) , Liu, Haiguang (jmhan@spin.yonsei.ac.kr (J.H.)) , Lee, Weontae (zyjin@spin.yonsei.ac.kr (Z.J.))

Abstract ▼ AI-Helper

HIV-1 integrase (HIV-1 IN) is an enzyme produced by the HIV-1 virus that integrates genetic material of the virus into the DNA of infected human cells. HIV-1 IN acts as a key component of the Retroviral Pre-Integration Complex (PIC). Protein dynamics could play an important role during the catalysis of HIV-1 IN; however, this process has not yet been fully elucidated. X-ray free electron laser (XFEL) together with nuclear magnetic resonance (NMR) could provide information regarding the dynamics during this catalysis reaction. Here, we report the non-cryogenic crystal structure of HIV-1 IN catalytic core domain at 2.5 Å using microcrystals in XFELs. Compared to the cryogenic structure at 2.1 Å using conventional synchrotron crystallography, there was a good agreement between the two structures, except for a catalytic triad formed by Asp64, Asp116, and Glu152 (DDE) and the lens epithelium-derived growth factor binding sites. The helix III region of the 140–153 residues near the active site and the DDE triad show a higher dynamic profile in the non-cryogenic structure, which is comparable to dynamics data obtained from NMR spectroscopy in solution state.

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Non-Cryogenic Structure and Dynamics of HIV-1 Integrase Catalytic Core Domain by X-ray Free-Electron Lasers 원문보기

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Non-Cryogenic Structure and Dynamics of HIV-1 Integrase Catalytic Core Domain by X-ray Free-Electron Lasers 원문보기

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