2adr | pdb_00002adr

ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES

spinqualitylabelsall models 2adr, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2adr is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ADR1_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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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