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

Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution.

Journal of molecular biology - 5 Feb 1999

Ibuka A, Taguchi A, Ishiguro M, Fushinobu S, Ishii Y, Kamitori S, Okuyama K, Yamaguchi K, Konno M, Matsuzawa H

Abstract excerpt

Bacterial resistance to beta-lactams is mainly due to the production of beta-lactamase. Especially through the production of extended-spectrum beta-lactamases (ESBLs), bacteria have acquired resistance not only to penicillins, but also to expanded-spectrum cephems. Here, we describe the crystal structure of the E166A mutant of class A beta-lactamase Toho-1 at 1.8 A resolution, the first reported tertiary...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9925786
DOI: 10.1006/jmbi.1998.2432

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution.PMID 9925786Read ↗

Improvement of crystal quality by surface mutations of beta-lactamase Toho-1.Semantic proximity Read ↗

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.Semantic proximity Read ↗

Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.Semantic proximity Read ↗

Structures of the Class D Carbapenemases OXA-23 and OXA-146: Mechanistic Basis of Activity against Carbapenems, Extended-Spectrum Cephalosporins, and AztreonamSemantic proximity Read ↗

Exploring the Mechanism of β-Lactam Ring Protonation in the Class A β-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography.Semantic proximity Read ↗

[Bacterial TEM-type serine beta-lactamases: structure and analysis of mutations].Semantic proximity Read ↗

The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.Semantic proximity Read ↗

Ultrahigh resolution structure of a class A beta-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme.Semantic proximity Read ↗

Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability.Semantic proximity Read ↗

Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.Semantic proximity Read ↗

A low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the β-lactamase BlaC.Semantic proximity Read ↗

Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp.Semantic proximity Read ↗

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