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2adr
From Proteopedia
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ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Overview
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.
About this Structure
2ADR is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Structure known Active Site: ZNC. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 17:35:04 2007
