6BR8
Structure of A6 reveals a novel lipid transporter
Summary for 6BR8
| Entry DOI | 10.2210/pdb6br8/pdb |
| Descriptor | Protein A6 homolog, [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate, (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, ... (4 entities in total) |
| Functional Keywords | poxvirus, a6, lipid binding, membrane biogenesis, viral protein |
| Biological source | Fowlpox virus (strain NVSL) (FPV) |
| Total number of polymer chains | 2 |
| Total formula weight | 66491.04 |
| Authors | Deng, J.,Peng, S.,Pathak, P. (deposition date: 2017-11-30, release date: 2018-06-20, Last modification date: 2024-11-20) |
| Primary citation | Pathak, P.K.,Peng, S.,Meng, X.,Han, Y.,Zhang, B.,Zhang, F.,Xiang, Y.,Deng, J. Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer. Proc. Natl. Acad. Sci. U.S.A., 115:7028-7032, 2018 Cited by PubMed Abstract: Cellular membranes are maintained as closed compartments, broken up only transiently during membrane reorganization or lipid transportation. However, open-ended membranes, likely derived from scissions of the endoplasmic reticulum, persist in vaccinia virus-infected cells during the assembly of the viral envelope. A group of viral membrane assembly proteins (VMAPs) were identified as essential for this process. To understand the mechanism of VMAPs, we determined the 2.2-Å crystal structure of the largest member, named A6, which is a soluble protein with two distinct domains. The structure of A6 displays a novel protein fold composed mainly of alpha helices. The larger C-terminal domain forms a unique cage that encloses multiple glycerophospholipids with a lipid bilayer-like configuration. The smaller N-terminal domain does not bind lipid but negatively affects lipid binding by A6. Mutations of key hydrophobic residues lining the lipid-binding cage disrupt lipid binding and abolish viral replication. Our results reveal a protein modality for enclosing the lipid bilayer and provide molecular insight into a viral machinery involved in generating and/or stabilizing open-ended membranes. PubMed: 29915071DOI: 10.1073/pnas.1805855115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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