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

Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.

Structure (London, England : 1993) - 15 Dec 1994

Liao D I, Herzberg O

Abstract excerpt

BACKGROUND: The histidine-containing phosphocarrier protein (HPr) functions in the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). His15 on HPr accepts a phosphoryl group from Enzyme I and transfers it to the Enzyme IIA domain of a sugar-specific PTS permease. In addition, HP...

Topics

Aspartic Acid
Bacterial Proteins
Binding Sites
Crystallography, X-Ray
Cysteine
Mutation
Phosphoenolpyruvate Sugar Phosphotransferase System
Protein Conformation
Protein Folding
Serine

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 7704530
DOI: 10.1016/s0969-2126(94)00122-7

Genes

PTS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7704530-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.PMID 7704530Read ↗

The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis.Semantic proximity Read ↗

Crystallization of the Bacillus subtilis histidine-containing phosphocarrier protein HPr and of some of its site-directed mutants.Semantic proximity Read ↗

Residual Helicity at the Active Site of the Histidine Phosphocarrier, HPr, Modulates Binding Affinity to Its Natural Partners.Semantic proximity Read ↗

Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system.Semantic proximity Read ↗

Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism.Semantic proximity Read ↗

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.Semantic proximity Read ↗

Solution structure of the IIAChitobiose-HPr complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.Semantic proximity Read ↗

Phenotypic consequences resulting from a methionine-to-valine substitution at position 48 in the HPr protein of Streptococcus salivarius.Semantic proximity Read ↗

Increased helix and protein stability through the introduction of a new tertiary hydrogen bond.Semantic proximity Read ↗

Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme.Semantic proximity Read ↗

Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution.Semantic proximity Read ↗

Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.Semantic proximity Read ↗

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