Molecular Playground/UreE

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Introduction

UreE is an essential metallochaperone for Helicobacter pylori (H.pylori). H.pylori is a class I human pathogen that is involved in causing gastric ulcers and stomach cancers. Its two nickel dependent enzymes - Urease and NiFe-H2ase, provides it a unique ability to survive and colonize in acidic human stomach. Urease catalyzes the conversion of urea to ammonia and carbamate which neutralizes its local acidic environment.

Function

Several accessory proteins play a crucial role in the maturation of Urease. UreE is a urease-specific nickel metallochaperone that is involved in the delivery nickel to urease.

Structural highlights

Apo-UreE from H.pylori is a dimer.HpUreE can bind one Ni(II) per dimer Nickel bound UreE. Nickel is bound to UreE in an octahedral fashion with one His from one subunit and two His from other subunit (UreE-Nickel Binding site).In presence of Ni, its oligomeric state changes to a tetramer (dimer of dimer).


References

<http://www.ncbi.nlm.nih.gov/pubmed/20681615/> [http://]

UreE complex with formate and Ni+2 ion (green) (PDB ID: 3tj8).

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Priyanka Basak, Alexander Berchansky

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