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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 19 Dec 2017

Yuen Man Hon, Fong Yu Hang, Nim Yap Shing, Lau Pak Ho, Wong Kam-Bo

Abstract excerpt

The ability of metallochaperones to allosterically regulate the binding/release of metal ions and to switch protein-binding partners along the metal delivery pathway is essential to the metallation of the metalloenzymes. Urease, catalyzing the hydrolysis of urea into ammonia and carbon dioxide, contains two nickel ions bound by a carbamylated lysine in its active site. Delivery of nickel ions for urease...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29203664
DOI: 10.1073/pnas.1712658114
PMCID: PMC5754787

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.PMID 29203664Read ↗

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