2BL6
Solution structure of the Zn complex of EIAV NCp11(22-58) peptide, including two CCHC Zn-binding motifs.
Summary for 2BL6
| Entry DOI | 10.2210/pdb2bl6/pdb |
| Related | 1EIA 1HEK 2EIA |
| NMR Information | BMRB: 7352 |
| Descriptor | NUCLEOCAPSID PROTEIN P11, ZINC ION (2 entities in total) |
| Functional Keywords | nucleocapsid protein, lentivirus, polyprotein, core protein, retrovirus zinc finger-like domains |
| Biological source | EQUINE INFECTIOUS ANEMIA VIRUS (EIAV) |
| Total number of polymer chains | 1 |
| Total formula weight | 4283.69 |
| Authors | Amodeo, P.,Castiglione-Morelli, M.A.,Ostuni, A.,Bavoso, A. (deposition date: 2005-03-02, release date: 2006-04-10, Last modification date: 2024-05-15) |
| Primary citation | Amodeo, P.,Castiglione-Morelli, M.A.,Ostuni, A.,Battistuzzi, G.,Bavoso, A. Structural Features in Eiav Ncp11: A Lentivirus Nucleocapsid Protein with a Short Linker Biochemistry, 45:5517-, 2006 Cited by PubMed Abstract: Lentiviral nucleocapsid proteins are a class of multifunctional proteins that play an essential role in RNA packaging and viral infectivity. They contain two CX(2)CX(4)HX(4)C zinc binding motifs connected by a basic linker of variable length. The 3D structure of a 37-aa peptide corresponding to sequence 22-58 from lentiviral EIAV nucleocapsid protein NCp11, complexed with zinc, has been determined by 2D (1)H NMR spectroscopy, simulated annealing, and molecular dynamics. The solution structure consists of two zinc binding domains held together by a five-residue basic linker Arg(38)-Ala-Pro-Lys-Val(42) that allows for spatial proximity between the two finger domains. Observed linker folding is stabilized by H bonded secondary structure elements, resulting in an Omega-shaped central region, asymmetrically centered on the linker. The conformational differences and similarities with other NC zinc binding knuckles have been systematically analyzed. The two CCHC motifs, both characterized by a peculiar Pro-Gly sequence preceding the His residue, although preserving Zn-binding geometry and chirality of other known NC proteins, exhibit local fold differences both between each other and in comparison with other previously characterized retroviral CCHC motifs. PubMed: 16634633DOI: 10.1021/BI0524924 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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