1a0a: Difference between revisions

Revision as of 15:42, 30 June 2008

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1a0a, resolution 2.80Å ()

Structural annotation:
Resources:	CATH : 1A0Aa00, 1A0Ab00 InterPro : Ipr011598, Ipr001092 Pfam : PF00010 SCOP : d1a0aa_, d1a0ab_ UniProt : P07270

Functional annotation:
Cellular component:	nucleus cytoplasm
Biological process:	regulation of transcription transcription phosphate metabolic process regulation of transcription, DNA-dependent cellular response to phosphate starvation
Molecular function:	DNA binding transcription regulator activity transcription factor activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

PHOSPHATE SYSTEM POSITIVE REGULATORY PROTEIN PHO4/DNA COMPLEXPHOSPHATE 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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Mon Jun 30 15:42:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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+===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]]
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