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CRYSTAL STRUCTURE OF PUT3/DNA COMPLEXCRYSTAL STRUCTURE OF PUT3/DNA COMPLEX
Structural highlights
Function[PUT3_YEAST] Positive activator of the proline utilization pathway. Binds to the promoters of PUT1 and PUT2 genes. Recognizes and binds to the DNA sequence 5'-CGG-N(10)-CCG-3'. 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 PubMedPUT3 is a member of a family of at least 79 fungal transcription factors that contain a six-cysteine, two-zinc domain called a 'Zn2Cys6 binuclear cluster'. We have determined the crystal structure of the DNA binding region from the PUT3 protein bound to its cognate DNA target. The structure reveals that the PUT3 homodimer is bound asymmetrically to the DNA site. This asymmetry orients a beta-strand from one protein subunit into the minor groove of the DNA resulting in a partial amino acid-base pair intercalation and extensive direct and water-mediated protein interactions with the minor groove of the DNA. These interactions facilitate a sequence dependent kink at the centre of the DNA site and specify the intervening base pairs separating two DNA half-sites that are contacted in the DNA major groove. A comparison with the GAL4-DNA and PPR1-DNA complexes shows how a family of related DNA binding proteins can use a diverse set of mechanisms to discriminate between the base pairs separating conserved DNA half-sites. Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster.,Swaminathan K, Flynn P, Reece RJ, Marmorstein R Nat Struct Biol. 1997 Sep;4(9):751-9. PMID:9303004[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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