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. 1997 Aug 1;16(15):4689–4697. doi: 10.1093/emboj/16.15.4689

Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition.

T Shimizu 1, A Toumoto 1, K Ihara 1, M Shimizu 1, Y Kyogoku 1, N Ogawa 1, Y Oshima 1, T Hakoshima 1
PMCID: PMC1170095  PMID: 9303313

Abstract

The crystal structure of a DNA-binding domain of PHO4 complexed with DNA at 2.8 A resolution revealed that the domain folds into a basic-helix-loop-helix (bHLH) motif with a long but compact loop that contains a short alpha-helical segment. This helical structure positions a tryptophan residue into an aromatic cluster so as to make the loop compact. PHO4 binds to DNA as a homodimer with direct reading of both the core E-box sequence CACGTG and its 3'-flanking bases. The 3'-flanking bases GG are recognized by Arg2 and His5. The residues involved in the E-box recognition are His5, Glu9 and Arg13, as already reported for bHLH/Zip proteins MAX and USF, and are different from those recognized by bHLH proteins MyoD and E47, although PHO4 is a bHLH protein.

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Selected References

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