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8VRH

E. coli peptidyl-prolyl cis-trans isomerase containing delta2-monofluoro-leucines

This is a non-PDB format compatible entry.
Summary for 8VRH
Entry DOI10.2210/pdb8vrh/pdb
DescriptorPeptidyl-prolyl cis-trans isomerase B, 1,2-ETHANEDIOL, TRIETHYLENE GLYCOL, ... (7 entities in total)
Functional Keywordspeptidyl-prolyl cis-trans isomerase, non-canonical amino acids, fluorinated leucine, isomerase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight74707.40
Authors
Frkic, R.L.,Jackson, C.J. (deposition date: 2024-01-22, release date: 2024-05-22, Last modification date: 2024-06-19)
Primary citationFrkic, R.L.,Tan, Y.J.,Abdelkader, E.H.,Maleckis, A.,Tarcoveanu, E.,Nitsche, C.,Otting, G.,Jackson, C.J.
Conformational Preferences of the Non-Canonical Amino Acids (2 S ,4 S )-5-Fluoroleucine, (2 S ,4 R )-5-Fluoroleucine, and 5,5'-Difluoroleucine in a Protein.
Biochemistry, 63:1388-1394, 2024
Cited by
PubMed Abstract: Proteins produced with leucine analogues, where CHF groups substitute specific methyl groups, can readily be probed by F NMR spectroscopy. As CF and CH groups are similar in hydrophobicity and size, fluorinated leucines are expected to cause minimal structural perturbation, but the impact of fluorine on the rotational freedom of CHF groups is unclear. We present high-resolution crystal structures of peptidyl-prolyl - isomerase B (PpiB) prepared with uniform high-level substitution of leucine by (2,4)-5-fluoroleucine, (2,4)-5-fluoroleucine, or 5,5'-difluoroleucine. Apart from the fluorinated leucine residues, the structures show complete structural conservation of the protein backbone and the amino acid side chains except for a single isoleucine side chain located next to a fluorine atom in the hydrophobic core of the protein. The carbon skeletons of the fluorinated leucine side chains are also mostly conserved. The CHF groups show a strong preference for staggered rotamers and often appear locked into single rotamers. Substitution of leucine CH groups for CHF groups is thus readily tolerated in the three-dimensional (3D) structure of a protein, and the rotation of CHF groups can be halted at cryogenic temperatures.
PubMed: 38742763
DOI: 10.1021/acs.biochem.4c00081
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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PDB entries from 2024-11-06

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