2adr
From Proteopedia
ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Structural highlights
FunctionADR1_YEAST Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. A folding transition and novel zinc finger accessory domain in the transcription factor ADR1.,Bowers PM, Schaufler LE, Klevit RE Nat Struct Biol. 1999 May;6(5):478-85. PMID:10331877[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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