3K4T
Crystal structure of the virion-associated protein P3 from caulimovirus
Summary for 3K4T
| Entry DOI | 10.2210/pdb3k4t/pdb |
| Related | 3F6N |
| Descriptor | Virion-associated protein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | coiled-coil, viral protein, tetramer, dna-binding protein, protein binding |
| Biological source | Cauliflower mosaic virus (STRAIN STRASBOURG) (CaMV) |
| Cellular location | Virion: P03551 |
| Total number of polymer chains | 4 |
| Total formula weight | 41992.02 |
| Authors | |
| Primary citation | Hoh, F.,Uzest, M.,Drucker, M.,Plisson-Chastang, C.,Bron, P.,Blanc, S.,Dumas, C. Structural insights into the molecular mechanisms of cauliflower mosaic virus transmission by its insect vector. J.Virol., 84:4706-4713, 2010 Cited by PubMed Abstract: Cauliflower mosaic virus (CaMV) is transmitted from plant to plant through a seemingly simple interaction with insect vectors. This process involves an aphid receptor and two viral proteins, P2 and P3. P2 binds to both the aphid receptor and P3, itself tightly associated with the virus particle, with the ensemble forming a transmissible viral complex. Here, we describe the conformations of both unliganded CaMV P3 protein and its virion-associated form. X-ray crystallography revealed that the N-terminal domain of unliganded P3 is a tetrameric parallel coiled coil with a unique organization showing two successive four-stranded subdomains with opposite supercoiling handedness stabilized by a ring of interchain disulfide bridges. A structural model of virus-liganded P3 proteins, folding as an antiparallel coiled-coil network coating the virus surface, was derived from molecular modeling. Our results highlight the structural and biological versatility of this coiled-coil structure and provide new insights into the molecular mechanisms involved in CaMV acquisition and transmission by the insect vector. PubMed: 20181714DOI: 10.1128/JVI.02662-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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