Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A Designed, Highly Efficient Pyrrolysyl-tRNA Synthetase Mutant Binds o-Chlorophenylalanine Using Two Halogen Bonds.

Journal of molecular biology - 30 Apr 2022

Vatansever Erol C, Yang Kai S, Geng Zhi Zachary, Qiao Yuchen, Li Pingwei, Xu Shiqing, Liu Wenshe Ray

Abstract excerpt

As one of the most valuable tools for genetic code expansion, pyrrolysyl-tRNA synthetase (PylRS) is structurally related to phenylalanyl-tRNA synthetase (PheRS). By introducing mutations that mimic ligand interactions in PheRS into PylRS, we designed a PylRS mutant. This mutant, designated as oClFRS, recognizes a number of o-substituted phenylalanines for their genetic incorporation at amber codon. Its efficiency...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acyl-tRNA Synthetases
Share to Genetic Code

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysine

Share to Mutation

Share to Phenylalanine

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 35278475
DOI: 10.1016/j.jmb.2022.167534
PMCID: PMC9018553

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Designed, Highly Efficient Pyrrolysyl-tRNA Synthetase Mutant Binds o-Chlorophenylalanine Using Two Halogen Bonds.PMID 35278475Read ↗

A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum.Semantic proximity Read ↗

Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function.Semantic proximity Read ↗

Two-Tier Screening Platform for Directed Evolution of Aminoacyl-tRNA Synthetases with Enhanced Stop Codon Suppression Efficiency.Semantic proximity Read ↗

The Pyrrolysyl-tRNA Synthetase Activity can be Improved by a P188 Mutation that Stabilizes the Full-Length Enzyme.Semantic proximity Read ↗

The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of L-phenylalanine and its derivatives.Semantic proximity Read ↗

Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant.Semantic proximity Read ↗

Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs.Semantic proximity Read ↗

Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency.Semantic proximity Read ↗

Structural Basis for the Specific Cotranslational Incorporation of p-Boronophenylalanine into Biosynthetic Proteins.Semantic proximity Read ↗

Thiol-yne radical reaction mediated site-specific protein labeling via genetic incorporation of an alkynyl-L-lysine analogue.Semantic proximity Read ↗

Continuous Hypermutation and Evolution of Noncanonical Amino Acid Synthases.Semantic proximity Read ↗

Stereochemical basis for engineered pyrrolysyl-tRNA synthetase and the efficient in vivo incorporation of structurally divergent non-native amino acids.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.