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

How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function

1 Oct 2013

Abstract excerpt

The expression of penicillin binding protein 2a (PBP2a) is the basis for the broad clinical resistance to the β-lactam antibiotics by methicillin-resistant Staphylococcus aureus (MRSA). The high-molecular mass penicillin binding proteins of bacteria catalyze in separate domains the transglycosylase and transpeptidase activities required for the biosynthesis of the peptidoglycan polymer that comprises the...

Read the complete abstract on PubMed

Topics

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

Share to Antibiotic Resistance in Bacteria
Share to Antimicrobial Resistance in Staphylococcus
Share to Microbial Natural Products and Biosynthesis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 24085846
DOI: 10.1073/pnas.1300118110

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological functionPMID 24085846Read ↗

Disruption of allosteric response as an unprecedented mechanism of resistance to antibiotics.Semantic proximity Read ↗

The basis for resistance to beta-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus.Semantic proximity Read ↗

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance.Semantic proximity Read ↗

Structural and kinetic analysis of the monofunctional Staphylococcus aureus PBP1Semantic proximity Read ↗

Thermosensitive PBP2a requires extracellular folding factors PrsA and HtrA1 for Staphylococcus aureus MRSA β-lactam resistanceSemantic proximity Read ↗

A Review on Five and Six-Membered Heterocyclic Compounds Targeting the Penicillin-Binding Protein 2 (PBP2A) of Methicillin-Resistant Staphylococcus aureus (MRSA)Semantic proximity Read ↗

A Review on Five and Six-Membered Heterocyclic Compounds Targeting the Penicillin-Binding Protein 2 (PBP2A) of Methicillin-Resistant <em>Staphylococcus aureus</em> (MRSA)Semantic proximity Read ↗

Computer-Aided Discovery of a β-Lactam-Independent Deep-Pocket PBP2a Binding Scaffold for Combating MRSA via Pharmacophore-Guided Scaffold Hopping and Bioisosteric ReplacementSemantic proximity Read ↗

Crystal structure of penicillin-binding protein 1a (PBP1a) reveals a mutational hotspot implicated in beta-lactam resistance in Streptococcus pneumoniae.Semantic proximity Read ↗

Exploring PBP2a resistance in MRSA by comparison between molecular covalent docking and non-covalent dockingSemantic proximity Read ↗

Structural Analysis of the Role of Pseudomonas aeruginosa Penicillin-Binding Protein 5 in β-Lactam ResistanceSemantic proximity Read ↗

A highly conserved interaction involving the middle residue of the SXN active-site motif is crucial for function of class B penicillin-binding proteins: mutational and computational analysis of PBP 2 from N. gonorrhoeae.Semantic proximity Read ↗

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