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<StructureSection load='1a0a' size='340' side='right'caption='[[1a0a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1a0a' size='340' side='right'caption='[[1a0a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a0a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1A0A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a0a]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=1a0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0a OCA], [https://pdbe.org/1a0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0a RCSB], [https://www.ebi.ac.uk/pdbsum/1a0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0a ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0a OCA], [https://pdbe.org/1a0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0a RCSB], [https://www.ebi.ac.uk/pdbsum/1a0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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.  
[https://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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=1a0a ConSurf].
</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/main_output.php?pdb_ID=1a0a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<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>
<div class="pdbe-citations 1a0a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Pho4|Pho4]]
*[[Pho4|Pho4]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hakoshima, T]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Ihara, K]]
[[Category: Hakoshima T]]
[[Category: Kyogoku, Y]]
[[Category: Ihara K]]
[[Category: Ogawa, N]]
[[Category: Kyogoku Y]]
[[Category: Oshima, Y]]
[[Category: Ogawa N]]
[[Category: Shimizu, M]]
[[Category: Oshima Y]]
[[Category: Shimizu, T]]
[[Category: Shimizu M]]
[[Category: Toumoto, A]]
[[Category: Shimizu T]]
[[Category: Basic helix loop helix]]
[[Category: Toumoto A]]
[[Category: Transcription factor]]
[[Category: Transcription-dna complex]]
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