1a0a: Difference between revisions

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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]]

Latest revision as of 09:26, 7 February 2024

PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEXPHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX

Structural highlights

1a0a is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1a0a, resolution 2.80Å

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OCA
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