Structure of a designed, right-handed coiled-coil tetramer containing all biological amino acids

@article{citeulike:1849911, abstract = {The previous design of an unprecedented family of two-, three-, and four-helical, right-handed coiled coils utilized nonbiological amino acids to efficiently pack spaces in the oligomer cores. Here we show that a stable, right-handed parallel tetrameric coiled coil, called RH4B, can be designed entirely using biological amino acids. The X-ray crystal structure of RH4B was determined to 1.1 A resolution using a designed metal binding site to coordinate a single Yb2+ ion per 33-amino acid polypeptide chain. The resulting experimental phases were particularly accurate, and the experimental electron density map provided an especially clear, unbiased view of the molecule. The RH4B structure closely matched the design, with equivalent core rotamers and an overall root-mean-square deviation for the N-terminal repeat of the tetramer of 0.24 A. The clarity and resolution of the electron density map, however, revealed alternate rotamers and structural differences between the three sequence repeats in the molecule. These results suggest that the RH4B structure populates an unanticipated variety of structures. 10.1110/ps.062702907}, author = {Sales, Mark and Plecs, Joseph J. and Holton, James M. and Alber, Tom }, citeulike-article-id = {1849911}, doi = {10.1110/ps.062702907}, journal = {Protein Sci}, keywords = {protein\_denovo\_design}, month = {October}, number = {10}, pages = {2224--2232}, posted-at = {2008-03-20 13:29:10}, priority = {2}, title = {Structure of a designed, right-handed coiled-coil tetramer containing all biological amino acids}, url = {http://dx.doi.org/10.1110/ps.062702907}, volume = {16}, year = {2007} }

TY - JOUR ID - citeulike:1849911 L3 - citeulike-article-id:1849911 TI - Structure of a designed, right-handed coiled-coil tetramer containing all biological amino acids JF - Protein Sci VL - 16 IS - 10 SP - 2224 EP - 2232 N2 - The previous design of an unprecedented family of two-, three-, and four-helical, right-handed coiled coils utilized nonbiological amino acids to efficiently pack spaces in the oligomer cores. Here we show that a stable, right-handed parallel tetrameric coiled coil, called RH4B, can be designed entirely using biological amino acids. The X-ray crystal structure of RH4B was determined to 1.1 A resolution using a designed metal binding site to coordinate a single Yb2+ ion per 33-amino acid polypeptide chain. The resulting experimental phases were particularly accurate, and the experimental electron density map provided an especially clear, unbiased view of the molecule. The RH4B structure closely matched the design, with equivalent core rotamers and an overall root-mean-square deviation for the N-terminal repeat of the tetramer of 0.24 A. The clarity and resolution of the electron density map, however, revealed alternate rotamers and structural differences between the three sequence repeats in the molecule. These results suggest that the RH4B structure populates an unanticipated variety of structures. 10.1110/ps.062702907 KW - protein_denovo_design AU - Sales, Mark AU - Plecs, Joseph AU - Holton, James AU - Alber, Tom PY - 2007/10/01/ UR - http://dx.doi.org/10.1110/ps.062702907 ER -