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Literature summary for 7.5.2.B8 extracted from

  • Albers, S.V.; Elferink,.MG.; Charlebois, R.L.; Sensen, C.W.; Driessen, A.J.; Konings, W.N.
    Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein (1999), J. Bacteriol., 181, 4285-4291.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution crystal structures of the enzyme in different states along its catalytic cycle: distinct monomeric nucleotide-free states and monomeric complexes with ADP-Mg2+ as a product-bound state, and with AMPPNP-Mg2+ as an ATP-like bound state. The structure of the enzyme consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ high-resolution structures of the enzyme–ADP-Mg2+ and GlcV–AMPPNP-Mg2+ complexes provide a detailed view of the residues involved in the binding of the nucleotide and the magnesium ion Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97UY8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + D-glucose/out
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Saccharolobus solfataricus ADP + phosphate + D-glucose/in
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Synonyms

Synonyms Comment Organism
ABC-ATPase GlcV
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Saccharolobus solfataricus