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

The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive.

Archives of biochemistry and biophysics - 15 Apr 2005

Pearson Josh T, Dabrowski Michael J, Kung Irene, Atkins William M

Abstract excerpt

Bacterial glutamine synthetases (GSs) are dodecameric aggregates comprised of two face-to-face hexameric rings, which form a cylindrical aqueous channel. Available crystal structures indicate that each subunit provides a 'central loop' that protrudes into this channel. Residues on either side of this loop contribute directly to substrate or metal ion cofactor binding. Although it has been suggested that this...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Disulfides
Share to Glutamate-Ammonia Ligase

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

Share to Magnesium

Share to Pyrenes

Share to Ribose

Share to Spectrometry, Fluorescence

Share to Spectrometry, Mass, Electrospray Ionization

Source

Identifiers

PMID: 15797252
DOI: 10.1016/j.abb.2005.02.008

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

The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive.PMID 15797252Read ↗

Molecular Mechanisms of Glutamine Synthetase Mutations that Lead to Clinically Relevant Pathologies.Semantic proximity Read ↗

Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase.Semantic proximity Read ↗

Q-SHINE: a versatile sensor for glutamine measurement via ligand-induced dimerizationSemantic proximity Read ↗

Structural and biophysical characterization of the tandem substrate-binding domains of the ABC importer GlnPQ.Semantic proximity Read ↗

Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Crystal structures capture three states in the catalytic cycle of a pyridoxal phosphate (PLP) synthase.Semantic proximity Read ↗

Activation and coupling of the glutaminase and synthase reaction of glutamate synthase is mediated by E1013 of the ferredoxin-dependent enzyme, belonging to loop 4 of the synthase domain.Semantic proximity Read ↗

Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase.Semantic proximity Read ↗

Characterisation of the conformational changes of GlnH that stimulate PknG activity in Mycobacteria and <i>Corynebacterium glutamicum</i>Semantic proximity Read ↗

The activation loop and substrate-binding cleft of glutaminase C are allosterically coupled.Semantic proximity Read ↗

Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase.Semantic proximity Read ↗

Understanding N-Acetyl-L-Glutamate Synthase Deficiency: Mutational Spectrum, Impact of Clinical Mutations on Enzyme Functionality, and Structural Considerations.Semantic proximity Read ↗

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