Crystal Structures of Apo and Metal-Bound Forms of the UreE Protein from Helicobacter pylori: Role of Multiple Metal Binding Sites
| Autor: | Abdalin Asinas, Miroslaw Cygler, Robert J. Maier, Allan Matte, Stéphane L. Benoit, Erica F. Miller, Christine Munger, Rong Shi |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Urease Protein Conformation Metal ions in aqueous solution Gene Expression chemistry.chemical_element Crystal structure Crystallography X-Ray Biochemistry Metal Apoenzymes Bacterial Proteins Tetramer Nickel Escherichia coli chemistry.chemical_classification Binding Sites Helicobacter pylori biology biology.organism_classification Crystallography Enzyme chemistry visual_art biology.protein visual_art.visual_art_medium Protein Multimerization Carrier Proteins Copper Protein Binding |
| Zdroj: | Biochemistry. 49:7080-7088 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | The crystal structure of the urease maturation protein UreE from Helicobacter pylori has been determined in its apo form at 2.1 A resolution, bound to Cu(2+) at 2.7 A resolution, and bound to Ni(2+) at 3.1 A resolution. Apo UreE forms dimers, while the metal-bound enzymes are arranged as tetramers that consist of a dimer of dimers associated around the metal ion through coordination by His102 residues from each subunit of the tetramer. Comparison of independent subunits from different crystal forms indicates changes in the relative arrangement of the N- and C-terminal domains in response to metal binding. The improved ability of engineered versions of UreE containing hexahistidine sequences at either the N-terminal or C-terminal end to provide Ni(2+) for the final metal sink (urease) is eliminated in the H102A version. Therefore, the ability of the improved Ni(2+)-binding versions to deliver more nickel is likely an effect of an increased local concentration of metal ions that can rapidly replenish transferred ions bound to His102. |
| Databáze: | OpenAIRE |
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