EC Number   |
Subunits |
Reference |
|---|
    2.7.7.60 | dimer |
gel filtration |
-, 726274 |
| 2.7.7.60 | dimer |
homodimer |
-, 393240, 393241, 393244 |
| 2.7.7.60 | dimer |
the beta-domains of the monomers are mainly responsible for the formation of the dimer |
-, 761358 |
| 2.7.7.60 | dimer |
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation |
-, 762421 |
| 2.7.7.60 | hexamer |
- |
656263 |
| 2.7.7.60 | hexamer |
6 * 41700, crystal structure analysis |
656263 |
| 2.7.7.60 | homodimer |
- |
-, 692926 |
| 2.7.7.60 | monomer |
sedimentation velocity experiments, both wild-type and mutant D152A |
672138 |
| 2.7.7.60 | More |
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview |
-, 762421 |
