2ADR
ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Summary for 2ADR
| Entry DOI | 10.2210/pdb2adr/pdb |
| Descriptor | ADR1, ZINC ION (2 entities in total) |
| Functional Keywords | transcription regulation, adr1, zinc finger |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P07248 |
| Total number of polymer chains | 1 |
| Total formula weight | 7257.01 |
| Authors | Bowers, P.M.,Kleivt, R.E. (deposition date: 1998-03-20, release date: 1998-06-17, Last modification date: 2024-05-22) |
| Primary citation | Bowers, P.M.,Schaufler, L.E.,Klevit, R.E. A folding transition and novel zinc finger accessory domain in the transcription factor ADR1. Nat.Struct.Biol., 6:478-485, 1999 Cited by PubMed Abstract: The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins. PubMed: 10331877DOI: 10.1038/8283 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
