2EBO
CORE STRUCTURE OF GP2 FROM EBOLA VIRUS
Summary for 2EBO
| Entry DOI | 10.2210/pdb2ebo/pdb |
| Descriptor | EBOLA VIRUS ENVELOPE GLYCOPROTEIN, CHLORIDE ION (3 entities in total) |
| Functional Keywords | envelope glycoprotein, filovirus, ebola virus, gp2, coat protein |
| Biological source | Zaire ebolavirus - Mayinga (Zaire, 1976) |
| Cellular location | GP2: Virion membrane ; Single-pass type I membrane protein . GP1: Virion membrane ; Peripheral membrane protein. GP2-delta: Secreted : Q05320 |
| Total number of polymer chains | 3 |
| Total formula weight | 25669.72 |
| Authors | Malashkevich, V.N.,Schneider, B.J.,Mcnally, M.L.,Milhollen, M.A.,Pang, J.X.,Kim, P.S. (deposition date: 1998-12-24, release date: 1999-05-18, Last modification date: 2024-10-30) |
| Primary citation | Malashkevich, V.N.,Schneider, B.J.,McNally, M.L.,Milhollen, M.A.,Pang, J.X.,Kim, P.S. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution. Proc.Natl.Acad.Sci.USA, 96:2662-2667, 1999 Cited by PubMed Abstract: Ebola virions contain a surface transmembrane glycoprotein (GP) that is responsible for binding to target cells and subsequent fusion of the viral and host-cell membranes. GP is expressed as a single-chain precursor that is posttranslationally processed into the disulfide-linked fragments GP1 and GP2. The GP2 subunit is thought to mediate membrane fusion. A soluble fragment of the GP2 ectodomain, lacking the fusion-peptide region and the transmembrane helix, folds into a stable, highly helical structure in aqueous solution. Limited proteolysis studies identify a stable core of the GP2 ectodomain. This 74-residue core, denoted Ebo-74, was crystallized, and its x-ray structure was determined at 1.9-A resolution. Ebo-74 forms a trimer in which a long, central three-stranded coiled coil is surrounded by shorter C-terminal helices that are packed in an antiparallel orientation into hydrophobic grooves on the surface of the coiled coil. Our results confirm the previously anticipated structural similarity between the Ebola GP2 ectodomain and the core of the transmembrane subunit from oncogenic retroviruses. The Ebo-74 structure likely represents the fusion-active conformation of the protein, and its overall architecture resembles several other viral membrane-fusion proteins, including those from HIV and influenza. PubMed: 10077567DOI: 10.1073/pnas.96.6.2662 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
