Beta propeller

Beta propeller 67,560, 764 Beta ribbons 241 Beta sheet 64 Beta spiral 74 Bicarbonate ion... 

Fulop, V., and Jones, D. T. (1999). Beta propellers Structural rigidity and functional diversity. Curr. Opin. Struct. Biol. 9, 715—721. 

Ma X, Panjikar S, Koepke J, Loris E, Stockigt J. The structure of 86. Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins. Plant Cell 2006 18 907-920. 

Sun S, Footer M, Matsudaira P. Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin. Mol Biol Cell 1997 8(3) 421-430. 

The WD-repeat-containing proteins form a very large family that is diverse in both its function and domain structure. Within all these proteins the WD-repeat domains are thought to have two common features the domain folds into a beta propeller and the domains form a platform without any catalytic activity on which multiple protein complexes assemble reversibly. The fact that these proteins play such key roles in the formation of protein-protein complexes in nearly all the major pathways and organelles unique to eukaryotic cells has two important implications. It supports both their ancient and proto eukaryotic origins and supports a likely association with many genetic diseases. 

Panchenko MP, Saxcna K, Li Y et al. Sites important for PLC beta(2) activation by the G protein beta gamma subunit map to the sides of the beta propeller structure. J Biol Chem 1998 273(43) 28298-304. 

Jing H, Takagi J, Liu JH ct al. Archaeal surface layer proteins contain beta propeller, PKD and beta helix domains and are related to metazoan cell surface proteins. Structiuc 2002 10(10) 1453-64. 

Pons T, Hernandez L, Batista FR ct al. Prediction of a common beta-propeller catalytic domain for fructosyltranferascs of different origin and substrate specificity. Protein Sci 2000 9 2285-91. 

Coronin-1 possesses 5 WD repeats and based on the homology with the G protein beta subunits it has been proposed that the WD repeat folds into a 5-bladed beta propeller. However, an extensive sequence analysis of coronin 1 revealed the presence of two additional sequence stretches of 46 and 44 residues, respectively, that flank the WD repeat-containing core sequence and are predicted to form four short P-strands and align with the corresponding P-strands of the five WD repeats. Since WD repeats are not strictly necessary to assert a propeller fold, the prediction suggests that the coronin 1 propeller domain is, in fact, made up of at least seven blades instead of the previously proposed five blades. Consistent with this analysis, the crystal structure of coronin 1 indeed revealed the presence of a 7-bladed propeller (see Fig. 1B,C). Furthermore, the presence of a 7-bladed propeller in coronin 1 is consistent with the predicted similarity between the coronin 1 N-terminal domain and the yeast transcriptional repressor Tupl as well as the G protein p-subunit, both WD repeat containing seven-bladed P-propeller proteins. 

Fulop V, Jones DT. Beta propellers structural rigidity and functional diversity. Curr Opin Struct Biol 1999 9(6) 715 721. 

Beta propellers. Another major folding pattern is a circular array of four to eight "blades" that form a propeller-like structure. Each blade is a small, roughly triangular four-stranded antiparallel P sheet (See Figs. 11-7 and 15-23). Sequences that fold into these blades can often, but not always, be recognized as WD repeats. These are typically 44- to 60-residue sequences that have the sequence GH (Gly-His) about 11-24 residues from the N terminus and WD (Trp-Asp) at the C terminus.This repeat sequence encodes the... 

A. Gaskell, S. Crennell, and G. Taylor, The three domains of a baeterial sialidase A beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure, 3 (1995) 1197—1205. 

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