Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori |
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| Authors: | Robert Lam Vladimir Romanov Kathy Johns Kevin P. Battaile Jean Wu‐Brown Jennifer L. Guthrie Robert P. Hausinger Emil F. Pai Nickolay Y. Chirgadze |
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| Affiliation: | 1. Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, Toronto, Ontario M5G 2C4, Canada;2. IMCA‐CAT, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439;3. Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan 48824;4. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824;5. Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada;6. Department of Medical Biophysics and Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada;7. Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ontario M5S 1A8, Canada |
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| Abstract: | ![]()
Urease plays a central role in the pathogenesis of Helicobacter pylori in humans. Maturation of this nickel metalloenzyme in bacteria requires the participation of the accessory proteins UreD (termed UreH in H. pylori), UreF, and UreG, which form sequential complexes with the urease apoprotein as well as UreE, a metallochaperone. Here, we describe the crystal structure of C‐terminal truncated UreF from H. pylori (residues 1–233), the first UreF structure to be determined, at 1.55 Å resolution using SAD methods. UreF forms a dimer in vitro and adopts an all‐helical fold congruent with secondary structure prediction. On the basis of evolutionary conservation analysis, the structure reveals a probable binding surface for interaction with other urease components as well as key conserved residues of potential functional relevance. Proteins 2010. © 2010 Wiley‐Liss, Inc. |
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| Keywords: | urease sequence conservation ConSurf protein– protein interactions dimer bacteria |
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