Structure of the ATP Binding Domain from the Archaeoglobus fulgidus Cu+-ATPase
نویسندگان
چکیده
منابع مشابه
CopB from Archaeoglobus fulgidus: a thermophilic Cu transporting CPx-ATPase
i ACKNOWLEDGEMENTS ii TABLE OF CONTENTS iii LIST OF FIGURES v LIST OF ABREVIATIONS vi
متن کاملCharacterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus.
The thermophilic, sulfur metabolizing Archaeoglobus fulgidus contains two genes, AF0473 and AF0152, encoding for PIB-type heavy metal transport ATPases. In this study, we describe the cloning, heterologous expression, purification, and functional characterization of one of these ATPases, CopA (NCB accession number AAB90763), encoded by AF0473. CopA is active at high temperatures (75 degrees C; ...
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P1B-type ATPases transport heavy metal ions across cellular membranes. Archaeoglobus fulgidus CopB is a member of this subfamily. We have cloned, expressed in Escherichia coli, and functionally characterized this enzyme. CopB and its homologs are distinguished by a metal binding sequence Cys-Pro-His in their sixth transmembrane segment (H6) and a His-rich N-terminal metal binding domain (His-N-...
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15 صفحه اولStructure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Conservation of energy based on the reduction of sulfate is of fundamental importance for the biogeochemical sulfur cycle. A key enzyme of this ancient anaerobic process is the dissimilatory sulfite reductase (dSir), which catalyzes the six-electron reduction of sulfite to hydrogen sulfide under participation of a unique magnetically coupled siroheme-[4Fe-4S] center. We determined the crystal s...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2006
ISSN: 0021-9258
DOI: 10.1074/jbc.m510708200