Cloned (Comment) | Organism |
---|---|
- |
Streptomyces avermitilis |
Crystallization (Comment) | Organism |
---|---|
complexes with the cofactors iron, alpha-ketoglutarate, and the nonreactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold and the cofactor-binding site for iron and alpha-keto-glutarate is similar to other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate | Streptomyces avermitilis |
Protein Variants | Comment | Organism |
---|---|---|
R117Q | complete loss of activity | Streptomyces avermitilis |
R188Q | 280fold decrease in activity | Streptomyces avermitilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces avermitilis | Q82IZ1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | no substrate: ent-1-deoxypentalenic acid | Streptomyces avermitilis | ? | - |
? |