Crystallization (Comment) | Organism |
---|---|
in complex with L-rhamnose, to 1.8 A resolution. Protein is a locally asymmetric dimer and has a preference for the beta-form of L-rhamnose | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
H22A | mutant does not fold properly | Escherichia coli |
H22K | mutant does not fold properly | Escherichia coli |
Y18A | mutant does not fold properly | Escherichia coli |
Y18E | mutant does not fold properly | Escherichia coli |
Y18F | binding affinity for L-rhamnose is comparable to that of the wild-type, no catalytic activity | Escherichia coli |
Y18H | mutant does not fold properly | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P32156 | - |
- |
General Information | Comment | Organism |
---|---|---|
physiological function | gene deletion leads o decreased growth rate only in the presence of low concentrations of L-rhamnose, with no difference in growth rate between the wild-type and mutant strains when the concentration of L-rhamnose in the media is 0.2%. The maximum amount of growth and the lag phase time of the wild-type strain are higher and shorter, respectively, compared with those of the mutant | Escherichia coli |