PHO4 bHLH结构域-DNA复合物的晶体结构：侧翼碱基识别
Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition.
作者信息
Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T
机构信息
Department of Molecular Biology, Nara Institute of Science and Technology, Ikoma, Japan.
出版信息
EMBO J. 1997 Aug 1;16(15):4689-97. doi: 10.1093/emboj/16.15.4689.
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.
摘要
以2.8埃分辨率解析的与DNA复合的PHO4 DNA结合结构域的晶体结构表明，该结构域折叠成一个碱性螺旋-环-螺旋（bHLH）基序，其环长但紧凑，包含一个短的α螺旋片段。这种螺旋结构将一个色氨酸残基定位到一个芳香族簇中，以使环紧凑。PHO4以同二聚体形式与DNA结合，直接读取核心E-box序列CACGTG及其3'侧翼碱基。3'侧翼碱基GG由Arg2和His5识别。参与E-box识别的残基是His5、Glu9和Arg13，这与之前报道的bHLH/Zip蛋白MAX和USF相同，并且与bHLH蛋白MyoD和E47识别的残基不同，尽管PHO4是一种bHLH蛋白。
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