Protein Variants | Comment | Organism |
---|---|---|
S67F | mutation in H-protein, significant decrease in activity | Escherichia coli |
S67P | mutation in H-protein, increase in activity | Escherichia coli |
S67Q | mutation in H-protein, significant decrease in activity | Escherichia coli |
S67T | mutation in H-protein, increase in activity | Escherichia coli |
S67V | mutation in H-protein, increase in activity | Escherichia coli |
S67Y | mutation in H-protein, significant decrease in activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6T9 | component H-protein | - |
General Information | Comment | Organism |
---|---|---|
physiological function | structure-based dynamic analysis of the induced release of the lipoate arm of protein H. Four major steps of the release process can be distinguished showing significantly different energy barriers and time scales. Mutations of key residue, Ser67 in protein H, leads to a bidirectional tuning of the release process | Escherichia coli |