Summary information and primary citation
- PDB-id
-
1a0a;
SNAP-derived features in text and
JSON formats
- Class
- transcription-DNA
- Method
- X-ray (2.8 Å)
- Summary
- Phosphate system positive regulatory protein pho4-DNA
complex
- Reference
-
Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y,
Ogawa N, Oshima Y, Hakoshima T (1997): "Crystal
structure of PHO4 bHLH domain-DNA complex: flanking base
recognition." EMBO J., 16,
4689-4697. 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.
