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 [1] or to the article describing Jmol [2] 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.
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:https://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
