Sandbox Reserved 1739

This Sandbox is Reserved from August 30, 2022 through May 31, 2023 for use in the course Biochemistry I taught by Kimberly Lane at the Radford University, Radford, VA, USA. This reservation includes Sandbox Reserved 1730 through Sandbox Reserved 1749.

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Hepatitis C Helicase/Primase

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function The function of Hepatitis C primase is to build the viral capsid. The viral capsid and two glycoproteins make up the genome (1). The function of Hepatitis C helicase is to stop viral RNA from binding by stripping it of its proteins. It is necessary for viral replication (2). Helicase can process a wide range of nucleic acid sequences and unwind them (5). Together, Hepatitis C primase and helicase function to ---- Disease Hepatitis C (HCV) is a viral infection that causes inflammation of the liver. As of 2022 there has been no vaccine created for Hepatitis C (6). Relevance The relevance of Hepatitis C helicase/primase is that the helicase/protease combination in HCV is believed to play a pivotal role in the replication cycle of HCV. The helicase exists as a dimer, bearing mutations, and can be found in three different functional states (9). The three functional states include a substrate-unbound state, an ATP-bound state, and an NA-bound state. The presence of ATP transitions the protease from high NA binding affinity to low NA binding affinity. The cooperation of helicase/protease binding the DNA is affected by the length of the ss lattice, and the desired ss DNA length is around 22nt (3). Structural highlights 2OBQ: for Hepatisis primase Method: X-Ray Diffraction. Resolution: 2.50 Å. Classification: Viral Protein. Organism(s): Hepacivirus C. Expression System: Escherichia coli. Deposited: 2006-12-19. Released: 2007-07-31. Deposition Author(s): Prongay, A.J., Guo, Z., Yao, N., Fischmann, T., Strickland, C., Myers Jr., J., Weber, P.C., Malcolm, B., Beyer, B.M., Ingram, R., Pichardo, J., Hong, Z., Prosise, W.W., Ramanathan, L., Taremi, S.S., Yarosh-Tomaine, T., Zhang, R., Senior, M., Yang, R., Arasappan, A., Bennett, F., Bogen, S.F., Chen, K., Jao, E., Liu, Y., Love, R.G., Saksena, A.K., Venkatraman, S., Girijavallabhan, V., Njoroge, F.G., Madison, V. Primary Structure: 180 amino acids. Secondary Structure (what types of secondary structure in the protein and number of each): Tertiary Structure(motif(s) present, domains): Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry): 8OHM for Hepatitis helicase: Method: X-Ray Diffraction. Resolution: 2.30 Å. Classification: Helicase. Organism(s): Hepacivirus C. Expression System: Escherichia coli BL21(DE3). Deposited: 1998-03-13. Released: 1999-04-20. Deposition Author(s): Cho, H.S., Ha, N.C., Kang, L.W., Oh, B.H. Primary Structure: 620 amino acids. Secondary Structure (what types of secondary structure in the protein and number of each): Beta sheets sandwiched between Alpha helices. Tertiary Structure(motif(s) present, domains): Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry): This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

[1]Gawlik, K.; Gallay, P. A. HCV Core Protein and Virus Assembly: What We Know without Structures. Immunologic research 2014, 60 (1), 1–10.

[2]Kolykhalov, A. A.; Mihalik, K.; Feinstone, S. M.; Rice, C. M. Hepatitis c Virus-Encoded Enzymatic Activities and Conserved RNA Elements in the 3′ Nontranslated Region Are Essential for Virus Replication in Vivo. Journal of Virology 2000, 74 (4), 2046–2051.

[3]Donmez, I.; Rajagopal, V.; Jeong, Y.-J.; Patel, S. S. Nucleic Acid Unwinding by Hepatitis c Virus and Bacteriophage T7 Helicases Is Sensitive to Base Pair Stability. Journal of Biological Chemistry 2007, 282 (29), 21116–21123.

[4]Turkington, C. Hepatitis C; McGraw-Hill/Contemporary, 1998.

[5]Rajagopal, V.; Gurjar, M.; Levin, M. K.; Patel, S. S. The Protease Domain Increases the Translocation Stepping Efficiency of the Hepatitis c Virus NS3-4A Helicase. Journal of Biological Chemistry 2010, 285 (23), 17821–17832.

[6]Locatelli, G. A.; Spadari, S.; Maga, G. Hepatitis c Virus NS3 ATPase/Helicase: An ATP Switch Regulates the Cooperativity among the Different Substrate Binding Sites†. Biochemistry 2002, 41 (32), 10332–10342.

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