1LE3

NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G

Replaces:  1HS0

Summary for 1LE3

• Entry DOI: 10.2210/pdb1le3/pdb
• Related: 1LE0 1LE1
• Descriptor: Tryptophan Zipper 4 (1 entity in total)
• Functional Keywords: beta-hairpin, type i beta-turn, protein binding
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654
• Total number of polymer chains: 1
• Total formula weight: 2012.09

Authors

Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A. (deposition date: 2002-04-09, release date: 2002-04-24, Last modification date: 2024-10-09)

Primary citation

Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A.
Tryptophan zippers: stable, monomeric beta -hairpins.
Proc.Natl.Acad.Sci.USA, 98:5578-5583, 2001

PubMed Abstract: A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks.

PubMed: 11331745
DOI: 10.1073/pnas.091100898

Experimental method

SOLUTION NMR