3FQM
Crystal structure of a novel dimeric form of HCV NS5A domain I protein
Summary for 3FQM
| Entry DOI | 10.2210/pdb3fqm/pdb |
| Related | 1ZH1 3FQQ |
| Descriptor | Non-structural protein 5A, ZINC ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | hcv, ns5a, domain i, phosphoprotein, rna-binding, metal binding protein |
| Biological source | Hepatitis C virus (isolate Con1) (HCV) |
| Total number of polymer chains | 2 |
| Total formula weight | 39159.09 |
| Authors | Love, R.A. (deposition date: 2009-01-07, release date: 2009-03-10, Last modification date: 2023-09-06) |
| Primary citation | Love, R.A.,Brodsky, O.,Hickey, M.J.,Wells, P.A.,Cronin, C.N. Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus J.Virol., 83:4395-4403, 2009 Cited by PubMed Abstract: A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly. PubMed: 19244328DOI: 10.1128/JVI.02352-08 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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