1YOD

Crystal structure of a water soluble analog of phospholamban

Summary for 1YOD

• Entry DOI: 10.2210/pdb1yod/pdb
• Descriptor: water-solublized phospholamban (2 entities in total)
• Functional Keywords: protein design, water-soluble, de novo protein
• Total number of polymer chains: 2
• Total formula weight: 7482.46

Authors

Slovic, A.M.,Stayrook, S.E.,North, B.,DeGrado, W.F. (deposition date: 2005-01-27, release date: 2005-04-19, Last modification date: 2024-11-20)

Primary citation

Slovic, A.M.,Stayrook, S.E.,North, B.,DeGrado, W.F.
X-ray structure of a water-soluble analog of the membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled coils.
J.Mol.Biol., 348:777-787, 2005

PubMed Abstract: Phospholamban (PLB) is a pentameric transmembrane protein that regulates the Ca(2+)-dependent ATPase SERCA2a in sarcoplasmic reticulum membranes. We previously described the computational design of a water-soluble variant of phospholamban, WSPLB, which reproduced many of the structural and functional properties of the native membrane-soluble protein. While the full-length WSPLB forms a pentamer in solution, a truncated variant forms very stable tetramers. To obtain insight into the tetramer-pentamer cytoplasmic switch, we solved the crystal structure of the truncated construct, WSPLB 21-52. This peptide has a heptad sequence repeat with Leu residues at a- and Ile at d-positions from residues 31-52. The crystal structure revealed that WSPLB 21-52 adopted an antiparallel tetrameric coiled coil. This topology contrasts with the parallel topology of an analogue of the coiled-coil of GCN4 with the same Leu(a) Ile(d) repeat. Analysis of these structures revealed how the nature of the partially exposed residues at e- and g-positions influence the topology formed by the bundle. We also constructed a model for the pentameric form of PLB using the coiled-coil parameters derived from a single monomer in the tetrameric structure. This model suggests that both buried and interfacial hydrogen bonds are important for stabilizing the parallel pentamer.

PubMed: 15826670
DOI: 10.1016/j.jmb.2005.02.040

Experimental method

X-RAY DIFFRACTION (1.8 Å)