| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10870962 | FEBS Letters | 2013 | 6 Pages |
Abstract
⺠Structure of the zinc-free DksA2 is similar to that of its zinc-finger paralog DksA. ⺠DksA2 binds in the RNA polymerase secondary channel. ⺠A disulfide bond formed by two DksA2 cysteines plays a minor role in DksA2 activity. ⺠Substitutions of the two cysteine residues destabilize DksA2 structure.
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Authors
Ran Furman, Tapan Biswas, Eric M. Danhart, Mark P. Foster, Oleg V. Tsodikov, Irina Artsimovitch,