1aw6: Difference between revisions

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==GAL4 (CD), NMR, 24 STRUCTURES==
==GAL4 (CD), NMR, 24 STRUCTURES==
<StructureSection load='1aw6' size='340' side='right' caption='[[1aw6]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
<StructureSection load='1aw6' size='340' side='right'caption='[[1aw6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1aw6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=125d 125d]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1aw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=125d 125d]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw6 OCA], [http://pdbe.org/1aw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw6 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw6 PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=1aw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw6 OCA], [https://pdbe.org/1aw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw6 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GAL4_YEAST GAL4_YEAST]] This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.  
[https://www.uniprot.org/uniprot/GAL4_YEAST GAL4_YEAST] This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw6_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Gal3-Gal80-Gal4|Gal3-Gal80-Gal4]]
*[[Gal3-Gal80-Gal4|Gal3-Gal80-Gal4]]
*[[Journal:JBIC:9|Journal:JBIC:9]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Baleja, J D]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Wagner, G]]
[[Category: Baleja JD]]
[[Category: Dna-binding]]
[[Category: Wagner G]]
[[Category: Transcription regulation]]

Latest revision as of 11:16, 22 May 2024

GAL4 (CD), NMR, 24 STRUCTURESGAL4 (CD), NMR, 24 STRUCTURES

Structural highlights

1aw6 is a 1 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 125d. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAL4_YEAST This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.

Evolutionary Conservation

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

Publication Abstract from PubMed

We have refined the solution structure of cadmium-bound GAL4 and present its 15N and 1H NMR assignments. The root-mean-square (rms) deviation to the average structure was 0.4 +/- 0.05 A for backbone atoms, and 0.9 +/- 0.1 A for all heavy atoms. The three-bond heteronuclear 3J(113Cd,1H) coupling constants were found to disobey a Karplus-type relationship, which was attributable to the unusual constraints imposed by the bimetal-thiolate cluster in GAL4. We conclude that the structural parameters that correlate to 3J(113Cd,1H) are complex.

Refined solution structure of the DNA-binding domain of GAL4 and use of 3J(113Cd,1H) in structure determination.,Baleja JD, Thanabal V, Wagner G J Biomol NMR. 1997 Dec;10(4):397-401. PMID:9460244[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Baleja JD, Thanabal V, Wagner G. Refined solution structure of the DNA-binding domain of GAL4 and use of 3J(113Cd,1H) in structure determination. J Biomol NMR. 1997 Dec;10(4):397-401. PMID:9460244
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