Beta helix

Schuler, B., Furst, F., Osterroth, F., Steinbacher, S., Huber, R., and Seckler, R. (2000). Plasticity and steric strain in a parallel beta-helix Rational mutations in the P22 tailspike protein. Proteins 39, 89-101. 

Lazo, N. D., and Downing, D. T. (1999). Crystalline regions of Bombyx mori silk fibroin may exhibit beta-turn and beta-helix conformations. Macromolecules 32, 4700-4705. Lee, K. H. (2004). Silk sericin retards the crystallization of silk fibroin. Macromol. Rapid Commun. 25, 1792-1796. 

Jenkins, J., Mayans, O., and Pickersgill, R. (1998). Structure and evolution of parallel beta-helix proteins. J. Struct. Biol. 122, 236-246. 

Junker, M., Schuster, C. C., McDonnell, A. V., Sorg, K. A., Finn, M. C., Berger, B., and Clark, P. L. (2006). Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc. Natl. Acad. Sci. USA 103, 4918-4923. 

Kajava, A. V., Cheng, N., Cleaver, R., Kessel, M., Simon, M. N., Willery, E., Jacob-Dubuisson, F., Locht, C., and Steven, A. C. (2001). Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. Mol. Microbiol. 42, 279-292. 

Kishimoto, A., Hasegawa, K., Suzuki, H., Taguchi, H., Namba, K., and Yoshida, M. (2004). Beta-helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem. Biophys. Res. Commun. 315, 739-745. 

Kisker, C., Schindelin, H., Alber, B. E., Ferry, J. G., and Rees, D. C. (1996). A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 15, 2323-2330. 

Liou, Y. C., Tocilj, A., Davies, P. L., andjia, Z. (2000). Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406, 322-324. 

Merlino, A., Esposito, L., and Vitagliano, L. (2006). Polyglutamine repeats and beta-helix structure Molecular dynamics study. Proteins 63(4), 918-927. 

Michel, G., Chantalat, L., Fanchon, E., Henrissat, B., Kloareg, B., and Dideberg, O. (2001). The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J. Biol. Chem. 276, 40202-40209. 

Petersen, T. N., Kauppinen, S., and Larsen, S. (1997). The crystal structure of rhamno-galacturonase A from Aspergillus aculeatus A right-handed parallel beta helix. Structure 5, 533-544. 

Raetz, C. R., and Roderick, S. L. (1995). A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyl transferase. Science 270, 997-1000. 

Smith, N. L., Taylor, E.J., Lindsay, A. M., Chamock, S.J., Turkenburg,J. P., Dodson, E.J., Davies, G. J., and Black, G. W. (2005). Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded beta-helix. Proc. Natl. Acad. Sci. USA 102, 17652-17657. 

Yoder, M. D., andjumak, F. (1995). Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J. 9, 335-342. 

Schuler, B., Rachel, R., and Seckler, R. (1999). Formation of fibrous aggregates from a non-native intermediate The isolated P22 tailspike beta-helix domain./. Biol. Chem. 274, 18589-18596. 

Figure 4.2 Crystal structure of potato tuber ADP-glucose small (catalytic) subunit monomer. The catalytic domain is in yellow and the beta-helix domain is in pink. ADPGlc is shown in atom type carbon atoms are green, oxygen atoms are red, nitrogen atoms are blue, phosphorus atoms are magenta, and the sulfate group is orange. (The full color version ofthis figure can be found atwww.Elsevier.books.com/)...

Figure 4.4 ADPGIc PPase monomer showing (a) the sulfate binding region between the catalytic and beta-helix domains and (b) the amino acid residues interacting with sulfate. The sulfate residues are yellow and the interacting residues are green in one subunit. The neighboring subunit and its residues are purple. (The full color version of this figure can be found atwww.Elsevier.books.com/)...

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. 

Attempts to use other features to classify the interfaces, such as the types of structural motifs of the protein (helix, beta, helix-turn-helix) or of the DNA (minor or major groove) involved in binding, have not yielded clear patterns thus far. More data on the structures of protein-DNA complexes are clearly needed in order to provide a better basis for performing classifications of the different types of protein-DNA complexes. 

Weigele PR, Haase-Pettingell C, Campbell PG, Gossard DC, King J (2005) Stalled folding mutants in the triple beta-helix domain of the phage P22 tailspike adhesion. J Mol Biol 354 1103-1117... 

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