7FDD

A Crystal structure of OspA mutant

Summary for 7FDD

• Entry DOI: 10.2210/pdb7fdd/pdb
• Descriptor: Outer surface protein A, DI(HYDROXYETHYL)ETHER (2 entities in total)
• Functional Keywords: outer surface protein a, lipid binding protein, lipoprotein
• Biological source: Borreliella burgdorferi
• Total number of polymer chains: 2
• Total formula weight: 51423.29

Authors

Shiga, S.,Makabe, K. (deposition date: 2021-07-16, release date: 2022-07-20, Last modification date: 2024-02-21)

Primary citation

Kiya, M.,Shiga, S.,Ding, P.,Koide, S.,Makabe, K.
beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking.
J.Mol.Biol., 436:168405-168405, 2024

PubMed Abstract: Domain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a β-hairpin sequence within a single-layer β-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two β-hairpin sequences with a Gly-Gly and shorteing of a β-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular β-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular β-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure.

PubMed: 38104859
DOI: 10.1016/j.jmb.2023.168405

Experimental method

X-RAY DIFFRACTION (2.9 Å)