3f6n
From Proteopedia
Crystal structure of the virion-associated protein P3 from Caulimovirus
Structural highlights
FunctionVAP_CAMVS Plays a role in virus cell-to-cell and plant-to-plant transmission. Interacts with virion icosahedral capsid and movement protein, thereby facilitating virion cell-to-cell transmission throug plasmodesmata opned by viral movement protein. Also interacts with aphid transmission factor, attaching the virion to aphid stylet when the animal feeds on an virus infected plant. Aphid saliva may later detach the virion, inducing release of infectious particles when the animal feeds on a new plant.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCauliflower 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. Structural insights into the molecular mechanisms of cauliflower mosaic virus transmission by its insect vector.,Hoh F, Uzest M, Drucker M, Plisson-Chastang C, Bron P, Blanc S, Dumas C J Virol. 2010 May;84(9):4706-13. Epub 2010 Feb 24. PMID:20181714[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
Categories: Large Structures | Blanc S | Dumas C | Hoh F | Uzest M