Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Desulfovibrio vulgaris |
Crystallization (Comment) | Organism |
---|---|
in complex with cobalt and sirohydrochlorin, to 1.7 A resolution | Desulfovibrio vulgaris |
Protein Variants | Comment | Organism |
---|---|---|
E184L | mutation in metal binding site, about 3fold increase in activity | Desulfovibrio vulgaris |
E184L/H216L | mutation in metal binding site, strong decrease in activity | Desulfovibrio vulgaris |
H154L | mutation in metal binding site. Mutant has negligible activity | Desulfovibrio vulgaris |
H154L/E184L | mutation in metal binding site, negligible activity | Desulfovibrio vulgaris |
H154L/E184L/H216L | mutation in metal binding site. Mutant has negligible activity | Desulfovibrio vulgaris |
H154L/H216L | mutation in metal binding site. Mutant has negligible activity | Desulfovibrio vulgaris |
H216L | mutation in metal binding site. Mutant has negligible activity | Desulfovibrio vulgaris |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Desulfovibrio vulgaris | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Desulfovibrio vulgaris | Q72EC8 | - |
- |
Desulfovibrio vulgaris DSM 644 | Q72EC8 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | sequence contains a 28 amino acid N-terminal signal peptide | Desulfovibrio vulgaris |
Synonyms | Comment | Organism |
---|---|---|
CbiKp | - |
Desulfovibrio vulgaris |
General Information | Comment | Organism |
---|---|---|
physiological function | residues His154 and His216 are essential for metal-chelation of sirohydrochlorin. The tetrameric form of the protein is stabilized by residues Arg54 and Glu76, which form hydrogen bonds between two subunits. His96 is responsible for the binding of two heme groups within the main central cavity of the tetramer. CbiKP binds two additional heme groups through interaction with His103 | Desulfovibrio vulgaris |