5YCT

Engineered hairpin loop3 mutant monomer in Single-chain Monellin

Summary for 5YCT

• Entry DOI: 10.2210/pdb5yct/pdb
• Descriptor: Single chain Monellin (2 entities in total)
• Functional Keywords: domain swapped dimer, single-chain monellin, loop mutation, qvvag motif, plant protein
• Biological source: Dioscoreophyllum cumminsii
• Total number of polymer chains: 2
• Total formula weight: 22986.25

Authors

Surana, P.,Nandwani, N.,Udgaonkar, J.B.,Gosavi, S.,Das, R. (deposition date: 2017-09-08, release date: 2018-11-28, Last modification date: 2023-11-22)

Primary citation

Nandwani, N.,Surana, P.,Negi, H.,Mascarenhas, N.M.,Udgaonkar, J.B.,Das, R.,Gosavi, S.
A five-residue motif for the design of domain swapping in proteins.
Nat Commun, 10:452-452, 2019

PubMed Abstract: Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two β-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse β-hairpin proteins.

PubMed: 30692525
DOI: 10.1038/s41467-019-08295-x

Experimental method

X-RAY DIFFRACTION (1.851 Å)