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Literature summary extracted from

  • Lübben, M.; Güldenhaupt, J.; Zoltner, M.; Deigweiher, K.; Haebel, P.; Urbanke, C.; Scheidig, A.J.
    Sulfate acts as phosphate analog on the monomeric catalytic fragment of the CPx-ATPase CopB from Sulfolobus solfataricus (2007), J. Mol. Biol., 369, 368-385.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.9 the catalytic fragment CopB-B is expressed in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.2.2.9 crystallization trials are performed at 18 °C by vapor diffusion using the hanging-drop technique, crystal structure of the catalytic fragment of a Sulfolobus solfataricus P-type ATPase, CopB-B, is determined with a 2.6 A resolution.In CopB-B crystals, a bound sulfate anion is identified at the phosphate-binding location. In solution state bound phosphate can be readily displaced by orthovanadate at submillimolar concentration as well as by sulfate at millimolar concentration. It is possible to assign the structure of the sulfate-bound phosphorylation domain of CopB-B to a state related to an enzyme/phosphate intermediate state of the catalytic cycle Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.9 Saccharolobus solfataricus Q97UU7 CopB
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Synonyms

EC Number Synonyms Comment Organism
7.2.2.9 CopB
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 Saccharolobus solfataricus
7.2.2.9 CPx-ATPase
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 Saccharolobus solfataricus