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Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of H...

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of H...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1458892267

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

About this item

Full title

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

Publisher

United States: Public Library of Science

Journal title

PLoS biology, 2013-10, Vol.11 (10), p.e1001678-e1001678

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation of a preactivation complex consisting of apo-urease and urease accessory proteins...

Alternative Titles

Full title

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1458892267

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1458892267

Other Identifiers

ISSN

1545-7885,1544-9173

E-ISSN

1545-7885

DOI

10.1371/journal.pbio.1001678

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