dGTP structure
This work was supported in part by funding from the Chinese Ministry of Science and Technology (number 2012CB911100 and number 2013ZX0001-005) and Chinese Ministry of Education (number IRT1016), the Key Laboratory of Molecular Virology, Jilin Province (20102209), China, and funding from Tianjin University.Chunfeng Zhu and Wenying Gao: These authors contributed equally to this workSchool of Life Sciences, Tianjin University, Tianjin, 300072, ChinaChunfeng Zhu, Xiaohong Qin, Xin Peng, Lei Zhang & Xiao-Fang YuInstitute of Virology and AIDS Research, First Hospital of Jilin University, 519 E Minzhu Avenue, Changchun, 130061, ChinaWenying Gao, Ke Zhao, Wenyan Zhang, Peng Li, Wei Wei & Xiao-Fang YuSchool of Life Sciences, Nankai University, Tianjin, 300072, ChinaBeijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing, 100049, ChinaDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, 615 North Wolfe Street, Baltimore, 21205, Maryland, USAYou can also search for this author in Nucleotide concentration is determined by measurements of absorbance at 257 nm. Hrecka, K. et al. You can also search for this author in McCoy, A. J. et al.
Ostertag, E. M., Prak, E. T., DeBerardinis, R. J., Moran, J. V. & Kazazian, H. H. Jr. You can also search for this author in Supplied in: Milli-Q® water as a lithium salt at (pH 7.0). Recent data also indicate that SAMHD1 regulates retrotransposition of LINE-1 elements. In the meantime, to ensure continued support, we are displaying the site without styles Nature Publishing Group 2019 Aug 30;47(4):1013-1027. doi: 10.1042/BST20180348. COVID-19 is an emerging, rapidly evolving situation. & Yu, X. F. Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFbeta and CRL5 E3 ubiquitin ligase components. Here we present the free-, ligand (dGTP)- and inhibitor (GTP)-bound structures of hexameric Ec- dGTPase, including an X-ray free-electron laser structure of the free Ec -dGTPase enzyme to 3.2 Å. Allosteric dGTP binding induces conformational changes at the active site, allowing a more stable interaction with the substrate and explaining the dGTP-induced SAMHD1 dNTPase activity. dGTP-triggered tetramer formation is also important for SAMHD1-mediated LINE-1 regulation. Thank you for visiting nature.com. DNA transfection was carried out using Lipofectamine 2000 (Invitrogen) according to the manufacturer’s instructions. and JavaScript.SAMHD1 is a dGTP-activated deoxynucleoside triphosphate triphosphohydrolase (dNTPase) whose dNTPase activity has been linked to HIV/SIV restriction. analysed the data. Mutations of dGTP binding residues in the allosteric site affect tetramer formation, dNTPase activity and HIV-1 restriction. You can also search for this author in & Kappes, J. C. Localization of the Vpx packaging signal within the C terminus of the human immunodeficiency virus type 2 Gag precursor protein. Functional analysis of the relationship between Vpx and the restriction factor SAMHD1. Nature Publishing Group Helices (A351–V378) from two separate subunits are linked by two dGTP molecules at both ends that are part of the allosteric sites. This site needs JavaScript to work properly. doi: 10.15252/embj.2019102931. The mechanism of its dGTP-activated dNTPase function remains unclear. 2020 Jun 23;11(1):3165. doi: 10.1038/s41467-020-16983-2.Husain A, Xu J, Fujii H, Nakata M, Kobayashi M, Wang JY, Rehwinkel J, Honjo T, Begum NA.EMBO J. and L.Z. All antibodies were used according to the manufacturers’ protocols.HEK293T cells were grown in DMEM medium with 10% FBS (Hyclone), GlutaMax and Pen-strep (Invitrogen). Modulation of LINE-1 and Alu/SVA retrotransposition by Aicardi-Goutieres syndrome-related SAMHD1. 2020 Aug 3;39(15):e102931. conceived and designed the overall project with valuable help from Y.G., Y.D., W.Z. Please enable it to take advantage of the complete set of features! A novel DCAF1-binding motif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest. To obtain Epub 2014 Oct 6.Proc Natl Acad Sci U S A.
dGTP binding in the allosteric site promotes the formation of the SAMHD1 tetramer and the conformational changes in the active site. Get the most important science stories of the day, free in your inbox. The interface is symmetric between the two chains around the axis (The substrate-binding pocket in the active site is formed by amino acids in the major lobe (Comparing the dGTP-bound tetramer complexed with substrate to the non-substrate-bound dimer (3U1N) revealed interesting structural differences.
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