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1a0a

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{{STRUCTURE_1a0a| PDB=1a0a | SCENE= }}
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'''PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX'''
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===PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9303313 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9303313}}
==About this Structure==
==About this Structure==
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[[Category: Basic helix loop helix]]
[[Category: Basic helix loop helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:42:46 2008''

Revision as of 12:42, 30 June 2008


PDB ID 1a0a

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1a0a, resolution 2.80Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX

Publication Abstract from PubMed

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.

Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition., Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T, EMBO J. 1997 Aug 1;16(15):4689-97. PMID:9303313

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1A0A is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition., Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T, EMBO J. 1997 Aug 1;16(15):4689-97. PMID:9303313

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