1yod: Difference between revisions

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[[Image:1yod.gif|left|200px]]
{{Seed}}
[[Image:1yod.png|left|200px]]


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{{STRUCTURE_1yod|  PDB=1yod  |  SCENE=  }}  
{{STRUCTURE_1yod|  PDB=1yod  |  SCENE=  }}  


'''Crystal structure of a water soluble analog of phospholamban'''
===Crystal structure of a water soluble analog of phospholamban===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15826670}}


==About this Structure==
==About this Structure==
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[[Category: Protein design]]
[[Category: Protein design]]
[[Category: Water-soluble]]
[[Category: Water-soluble]]
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