Sandbox Reserved 1739

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== Function ==
== Function ==
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The function of Hepatitis C primase is to build the viral capsid. The viral capsid and two glycoproteins make up the genome (1).
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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).
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Together, Hepatitis C primase and helicase function to ----
== Disease ==
== Disease ==
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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 ==
== Relevance ==
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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 ==
== Structural highlights ==
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2OBQ: for Hepatisis primase
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Method: X-Ray Diffraction.
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Resolution: 2.50 Å.
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Classification: Viral Protein.
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Organism(s): Hepacivirus C.
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Expression System: Escherichia coli.
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Deposited: 2006-12-19.
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Released: 2007-07-31.
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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.
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Primary Structure: 180 amino acids.
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Secondary Structure (what types of secondary structure in the protein and number of each):
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Tertiary Structure(motif(s) present, domains):
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Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry):
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8OHM for Hepatitis helicase:
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Method: X-Ray Diffraction.
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Resolution: 2.30 Å.
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Classification: Helicase.
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Organism(s): Hepacivirus C.
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Expression System: Escherichia coli BL21(DE3).
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Deposited: 1998-03-13.
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Released: 1999-04-20.
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Deposition Author(s): Cho, H.S., Ha, N.C., Kang, L.W., Oh, B.H.
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Primary Structure: 620 amino acids.
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Secondary Structure (what types of secondary structure in the protein and number of each): Beta sheets sandwiched between Alpha helices.
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Tertiary Structure(motif(s) present, domains):
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Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry):
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
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<references/>
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[1]Gawlik, K.; Gallay, P. A. HCV Core Protein and Virus Assembly: What We Know without Structures. Immunologic research 2014, 60 (1), 1–10.
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[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.
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[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.
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[4]Turkington, C. Hepatitis C; McGraw-Hill/Contemporary, 1998.
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[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.
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[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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Revision as of 06:07, 15 November 2022

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

Caption for this structure

Drag the structure with the mouse to rotate

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.

[7] [8] [9] [10]

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