5H3D
Helical structure of membrane tubules decorated by ACAP1 (BARPH doamin) protein by cryo-electron microscopy and MD simulation
Summary for 5H3D
| Entry DOI | 10.2210/pdb5h3d/pdb |
| EMDB information | 2546 |
| Descriptor | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (1 entity in total) |
| Functional Keywords | acap1 barph domain, membrane remodeling, molecular dynamics simulation, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 173337.39 |
| Authors | Chan, C.,Pang, X.Y.,Zhang, Y.,Sun, F.,Fan, J. (deposition date: 2016-10-22, release date: 2019-01-16, Last modification date: 2024-03-20) |
| Primary citation | Chan, C.,Pang, X.,Zhang, Y.,Niu, T.,Yang, S.,Zhao, D.,Li, J.,Lu, L.,Hsu, V.W.,Zhou, J.,Sun, F.,Fan, J. ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages. Plos Comput.Biol., 15:e1007081-e1007081, 2019 Cited by PubMed Abstract: Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) into an unusual lattice structure that also uncovers a new paradigm for how a BAR protein deforms membrane. Here, we initially pursued computation-based refinement of the ACAP1 lattice to identify its critical protein contacts. Simulation studies then revealed how ACAP1, which dimerizes into a symmetrical structure in solution, is recruited asymmetrically to the membrane through dynamic behavior. We also pursued electron microscopy (EM)-based structural studies, which shed further insight into the dynamic nature of the ACAP1 lattice assembly. As ACAP1 is an unconventional BAR protein, our findings broaden the understanding of the mechanistic spectrum by which proteins assemble into higher-ordered structures to achieve membrane deformation. PubMed: 31291238DOI: 10.1371/journal.pcbi.1007081 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (14 Å) |
Structure validation
Download full validation report
