3PLT

Crystal structure of Lsp1 from Saccharomyces cerevisiae

Summary for 3PLT

Entry DOI	10.2210/pdb3plt/pdb
Descriptor	Sphingolipid long chain base-responsive protein LSP1 (2 entities in total)
Functional Keywords	eisosomes, lsp1, pil1, bar domain, plasma membrane, self-assembly, phosphoprotein, structural protein
Biological source	Saccharomyces cerevisiae (yeast)
Cellular location	Cytoplasm, cell cortex: Q12230
Total number of polymer chains	3
Total formula weight	78244.08
Authors	Ziolkowska, N.E.,Walther, T.C. (deposition date: 2010-11-15, release date: 2011-06-22, Last modification date: 2024-02-21)
Primary citation	Ziolkowska, N.E.,Karotki, L.,Rehman, M.,Huiskonen, J.T.,Walther, T.C. Eisosome-driven plasma membrane organization is mediated by BAR domains. Nat.Struct.Mol.Biol., 18:854-856, 2011 Cited by PubMed Abstract: Plasma membranes are organized into domains of different protein and lipid composition. Eisosomes are key complexes for yeast plasma membrane organization, containing primarily Pil1 and Lsp1. Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization. PubMed: 21685922 DOI: 10.1038/nsmb.2080 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.9 Å)

Structure validation