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Literature summary for 2.8.4.3 extracted from
- Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein (2002), J. Biol. Chem., 277, 13367-13370.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 53600 | - |
1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein | Escherichia coli |
| 60000 | - |
gel filtration, His-tagged recombinan protein | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AEI1 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| [4Fe-4S]-center | enzyme MiaB contains both iron and sulfide and an apoprotein form can chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per polypeptide chain. Under reducing and anaerobic conditions, a [4Fe-4S] cluster is present, whereas [2Fe-2S] and [3Fe-4S] forms are generated under aerobic conditions. Residues Cys157, Cys161, and Cys164 are involved in iron chelation, and the cluster is essential for activity | Escherichia coli |  |
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