6LJI

X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11V

Summary for 6LJI

• Entry DOI: 10.2210/pdb6lji/pdb
• Related: 6L91 6L9B 6L9D
• Descriptor: Immunoglobulin G-binding protein G (2 entities in total)
• Functional Keywords: synthetic gb1 domain variant, d-aminoacid substitution, immune system
• Biological source: Streptococcus sp. group G
• Total number of polymer chains: 2
• Total formula weight: 12307.31

Authors

Penmatsa, A.,Chatterjee, J.,Majumder, P.,Khatri, B. (deposition date: 2019-12-16, release date: 2020-08-12, Last modification date: 2024-10-23)

Primary citation

Khatri, B.,Majumder, P.,Nagesh, J.,Penmatsa, A.,Chatterjee, J.
Increasing protein stability by engineering the n -> pi * interaction at the beta-turn.
Chem Sci, 11:9480-9487, 2020

PubMed Abstract: Abundant n → π* interactions between adjacent backbone carbonyl groups, identified by statistical analysis of protein structures, are predicted to play an important role in dictating the structure of proteins. However, experimentally testing the prediction in proteins has been challenging due to the weak nature of this interaction. By amplifying the strength of the n → π* interaction amino acid substitution and thioamide incorporation at a solvent exposed β-turn within the proteins and Pin 1 WW domain, we demonstrate that an n → π* interaction increases the structural stability of proteins by restricting the torsion angle. Our results also suggest that amino acid side-chain identity and its rotameric conformation play an important and decisive role in dictating the strength of an n → π* interaction.

PubMed: 34094214
DOI: 10.1039/d0sc03060k

Experimental method

X-RAY DIFFRACTION (1.843 Å)