Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6L9D

X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11S

Summary for 6L9D
Entry DOI10.2210/pdb6l9d/pdb
DescriptorImmunoglobulin G-binding protein G (2 entities in total)
Functional Keywordssynthetic gb1 domain variant, d-aminoacid substitution, immune system
Biological sourceStreptococcus sp. group G
Total number of polymer chains1
Total formula weight6141.60
Authors
Penmatsa, A.,Chatterjee, J.,Majumder, P.,Khatri, B. (deposition date: 2019-11-08, release date: 2020-08-12, Last modification date: 2024-11-13)
Primary citationKhatri, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.73 Å)
Structure validation

229380

PDB entries from 2024-12-25

PDB statisticsPDBj update infoContact PDBjnumon