1a0a: Difference between revisions

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[[Image:1a0a.~~gif~~|left|200px]]

[[Image:1a0a.png|left|200px]]

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~~'''~~PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX~~'''~~

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

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9303313}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9303313 is the PubMed ID number.

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==About this Structure==

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[[Category: Basic helix loop helix]]

[[Category: Transcription factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 09~~:36:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:42:46 2008''

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-[[Image:1a0a.gif|left|200px]]
+{{Seed}}
+[[Image:1a0a.png|left|200px]]
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 {{STRUCTURE_1a0a|  PDB=1a0a  |  SCENE=  }}
-'''PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX'''
+===PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEX===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9303313}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9303313 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9303313}}
 ==About this Structure==
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 [[Category: Basic helix loop helix]]
 [[Category: Transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:36:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:42:46 2008''