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Literature summary for 7.6.2.8 extracted from
- Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF (2012), FEBS Lett., 586, 972-976.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| catalytically impaired BtuCD mutant E159Q in complex with BtuF, to 3.5 A resolution. The BtuC subunits adopts a distinct asymmetric conformation. The structure suggests that BtuF does not discriminate between, or impose, asymmetric conformations of BtuCD | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E159Q | mutation in subunit BtuD, results in abolished ATP hydrolysis activity of BtuCDF. Mutant is still able to bind nucleotides and binding protein BtuF in a manner similar to the wild-type protein | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inner membrane | - |
Escherichia coli | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
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Release 2023.1 (January 2023)
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