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

Nickel Ligation of the N-Terminal Amine of HypA Is Required for Urease Maturation in Helicobacter pylori.

Biochemistry - 28 Feb 2017

Hu Heidi Q, Johnson Ryan C, Merrell D Scott, Maroney Michael J

Abstract excerpt

The human pathogen Helicobacter pylori requires nickel for colonization of the acidic environment of the stomach. HypA, a Ni metallochaperone that is typically associated with hydrogenase maturation, is also required for urease maturation and acid survival of H. pylori. There are two proposed Ni site structures for HypA; one is a paramagnetic six-coordinate site characterized by X-ray absorption spectroscopy...

Read the complete abstract on PubMed

Topics

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

Share to Amines
Share to Carrier Proteins
Share to Helicobacter pylori

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Nickel

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Share to Urease

Source

Open in PubMed Open full text

Identifiers

PMID: 28177601
DOI: 10.1021/acs.biochem.6b00912
PMCID: PMC5540134

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nickel Ligation of the N-Terminal Amine of HypA Is Required for Urease Maturation in Helicobacter pylori.PMID 28177601Read ↗

Dynamic HypA zinc site is essential for acid viability and proper urease maturation in Helicobacter pylori.Semantic proximity Read ↗

Nickel translocation between metallochaperones HypA and UreE in Helicobacter pyloriSemantic proximity Read ↗

Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori.Semantic proximity Read ↗

Nickel trafficking system responsible for urease maturation inHelicobacter pyloriSemantic proximity Read ↗

Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pyloriSemantic proximity Read ↗

Evolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for ColonizationSemantic proximity Read ↗

Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.Semantic proximity Read ↗

Structural insights into how metallochaperones UreE and UreG interact to deliver a toxic metal to ureaseSemantic proximity Read ↗

Nickel enzyme maturation in Helicobacter hepaticus: roles of accessory proteins in hydrogenase and urease activities.Semantic proximity Read ↗

Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.Semantic proximity Read ↗

The <i>Helicobacter pylori</i> GroES Cochaperonin HspA Functions as a Specialized Nickel Chaperone and Sequestration Protein through Its Unique C-Terminal ExtensionSemantic proximity Read ↗

UreE-UreG Complex Facilitates Nickel Transfer and Preactivates GTPase of UreG in Helicobacter pyloriSemantic proximity Read ↗

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