2OYB

The crystal structure of OspA mutant

Summary for 2OYB

• Entry DOI: 10.2210/pdb2oyb/pdb
• Related: 2OY1 2OY5 2OY7 2OY8
• Descriptor: Outer surface protein A (2 entities in total)
• Functional Keywords: beta-sheet, membrane protein
• Biological source: Borrelia burgdorferi (Lyme disease spirochete)
• Total number of polymer chains: 1
• Total formula weight: 26571.58

Authors

Makabe, K.,Biancalana, M.,Terechko, V.,Koide, S. (deposition date: 2007-02-21, release date: 2008-03-04, Last modification date: 2023-08-30)

Primary citation

Biancalana, M.,Makabe, K.,Koide, A.,Koide, S.
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics
J.Mol.Biol., 383:205-213, 2008

PubMed Abstract: Though beta-rich self-assemblies comprise a major structural class of polypeptides, a detailed understanding of the determinants of their structure and stability is lacking. In particular, the roles of repetitive stretches of side chains running the long axis of these beta-sheets, termed "cross-strand ladders," remain poorly characterized due to the inherently insoluble and heterogeneous nature of self-assemblies. To overcome these experimental challenges, we have established a complementary experimental system termed "peptide self-assembly mimics" (PSAMs). The PSAMs capture a defined number of self-assembly-like peptide repeats within a soluble beta-rich protein, making structural and energetic studies possible. In this work, we investigated the role of cross-strand ladders containing aromatic residues, which are prominent in self-assembling peptides. A combination of solution data and high-resolution crystal structures revealed that a single cross-strand ladder consisting solely of Tyr significantly stabilized, rigidified, and flattened the PSAM beta-sheet. These characteristics would stabilize each beta-sheet layer of a self-assembly and direct sheet conformations compatible with lamination. Our results therefore provide a rationale for the abundance of aromatic amino acids in fibril-forming peptides and establish important roles of cross-strand Tyr ladders in the structure and stability of beta-rich peptide self-assemblies.

PubMed: 18762191
DOI: 10.1016/j.jmb.2008.08.031

Experimental method

X-RAY DIFFRACTION (1.3 Å)