1a0a

<StructureSection load='1a0a' size='340' side='right' caption='[[1a0a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1a0a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0A FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0a RCSB], [http://www.ebi.ac.uk/pdbsum/1a0a PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PHO4_YEAST PHO4_YEAST]] Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/1a0a_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== 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<ref>PMID:9303313</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Pho4 bHLH Protein|Pho4 bHLH Protein]]

[[Category: Hakoshima, T]]

[[Category: Ihara, K]]

[[Category: Kyogoku, Y]]

[[Category: Ogawa, N]]

[[Category: Oshima, Y]]

[[Category: Shimizu, M]]

[[Category: Shimizu, T]]

[[Category: Toumoto, A]]

[[Category: Transcription-dna complex]]