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| - | [[Image:1zw8.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1zw8.png|left|200px]] |
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| | {{STRUCTURE_1zw8| PDB=1zw8 | SCENE= }} | | {{STRUCTURE_1zw8| PDB=1zw8 | SCENE= }} |
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| - | '''Solution structure of a ZAP1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae'''
| + | ===Solution structure of a ZAP1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae=== |
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| - | ==Overview==
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| - | The Zap1 transcription factor controls expression of genes that regulate zinc homeostasis in Saccharomyces cerevisiae. The solution structure of two zinc fingers (zf1-2(CA3)) derived from a zinc-responsive domain of Zap1 (zf1-2) has been determined. Under zinc-limiting conditions, zinc finger 2 (zf2) from this domain has been shown to be a constitutive transcriptional activator. Moreover, repression of zf2 function in zinc-replete cells required zinc coordination to both canonical finger 1 (zf1) and zf2 metal sites, suggesting zf1-zf2 cooperativity underlies Zap1 metalloregulation. A structural basis for this cooperativity is identified here. Favorable inter-helical contacts in zf1-2(CA3) extend the individual finger hydrophobic cores through the zf1-zf2 interface. Tryptophan residues at position 5 in each finger provide numerous non-helical inter-finger contacts reminiscent of those observed in GLI1 zinc fingers 1 and 2. The molecular mechanism for zf1-dependent repression of zf2 transcriptional activation is explored further using NMR and CD titration studies. While zf1 independently forms a betabetaalpha solution structure, the majority of zf2 ensemble solution states do not adopt the canonical betabetaalpha zinc finger fold without zf1-zf2 interactions. Cooperative effects on Zn(II) affinities stemming from these finger-finger interactions are observed also in calorimetric studies, in which the 160(+/-20)nM (zf1) and 250(+/-40)nM (zf2) K(d) values for each individual finger increased substantially in the context of the zf1-2 protein (apparent K(dzf1-2WT)=4.6(+/-1.2)nM). On the basis of the above observations, we propose a mechanism for Zap1 transcriptional regulation in which zf1-zf2 interactions stabilize the betabetaalpha folded "repressed state" of the zf2 activation domain in the presence of cellular Zn(II) excess. Moreover, in contrast to earlier reports of <<1 labile zinc ion/Escherichia coli cell, the zf1-zf2 zinc affinities determined calorimetrically are consistent with Zn(II) levels >>1 labile zinc ion/eukaryotic cell. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16483601}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16483601 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16483601}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1ZW8 is a [[Single protein]] structure of 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=1ZW8 OCA]. | + | 1ZW8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZW8 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Nmr solution structure]] | | [[Category: Nmr solution structure]] |
| | [[Category: Zap1]] | | [[Category: Zap1]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:09:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:09:08 2008'' |
Revision as of 07:09, 28 July 2008
Template:STRUCTURE 1zw8
Solution structure of a ZAP1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae
Template:ABSTRACT PUBMED 16483601
About this Structure
1ZW8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.
Reference
Solution structure of a Zap1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae., Wang Z, Feng LS, Matskevich V, Venkataraman K, Parasuram P, Laity JH, J Mol Biol. 2006 Apr 7;357(4):1167-83. Epub 2006 Jan 24. PMID:16483601
Page seeded by OCA on Mon Jul 28 10:09:08 2008
