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

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

Journal of molecular biology - 5 Mar 1990

Kapadia G, Reizer J, Sutrina S L, Saier M H, Reddy P, Herzberg O

Abstract excerpt

The histidine-containing phosphocarrier protein (HPr) from Bacillus subtilis has been crystallized. Two of the site-directed mutants aimed at probing function produce crystals suitable for X-ray studies. The mutant in which His15 is substituted by an alanyl residue crystallizes from ammonium sulfate solution in space group P3(1)21 or P3(2)21, with unit cell dimensions: a = b = 47.3 A; c = 61.5 A. These crystals...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Bacterial Proteins

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

Share to Crystallization

Share to Mutation

Share to Phosphoenolpyruvate Sugar Phosphotransferase System

Share to Polyethylene Glycols

Share to X-Ray Diffraction

Source

Identifiers

PMID: 2108249
DOI: 10.1016/0022-2836(90)90296-X

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

Crystallization of the Bacillus subtilis histidine-containing phosphocarrier protein HPr and of some of its site-directed mutants.PMID 2108249Read ↗

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

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

Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus.Semantic proximity Read ↗

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

Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC.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 ↗

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

Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification.Semantic proximity Read ↗

Regulatory protein phosphorylation in Mycoplasma pneumoniae. A PP2C-type phosphatase serves to dephosphorylate HPr(Ser-P).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 ↗

Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution.Semantic proximity Read ↗

The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression.Semantic proximity Read ↗

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