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| | ==NMR Structure of the ZFY-6T[Y10L] Zinc Finger== | | ==NMR Structure of the ZFY-6T[Y10L] Zinc Finger== |
| - | <StructureSection load='1kls' size='340' side='right'caption='[[1kls]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1kls' size='340' side='right'caption='[[1kls]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kls]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KLS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KLS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5znf|5znf]], [[1klr|1klr]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1kls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kls OCA], [http://pdbe.org/1kls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kls RCSB], [http://www.ebi.ac.uk/pdbsum/1kls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kls ProSAT]</span></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=1kls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kls OCA], [https://pdbe.org/1kls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kls RCSB], [https://www.ebi.ac.uk/pdbsum/1kls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kls ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZFY_HUMAN ZFY_HUMAN]] Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. | + | [https://www.uniprot.org/uniprot/ZFY_HUMAN ZFY_HUMAN] Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lachenmann, M J]] | + | [[Category: Lachenmann MJ]] |
| - | [[Category: Ladbury, J E]] | + | [[Category: Ladbury JE]] |
| - | [[Category: Narayana, N]] | + | [[Category: Narayana N]] |
| - | [[Category: Phillips, N B]] | + | [[Category: Phillips NB]] |
| - | [[Category: Qian, X]] | + | [[Category: Qian X]] |
| - | [[Category: Weiss, M A]] | + | [[Category: Weiss MA]] |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
ZFY_HUMAN Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'.
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
The Zn finger provides a model for studies of protein structure and stability. Its core contains a conserved phenylalanine residue adjoining three architectural elements: a beta-hairpin, an alpha-helix and a tetrahedral Zn(2+)-binding site. Here, we demonstrate that the consensus Phe is not required for high-affinity Zn(2+) binding but contributes to the specification of a precise DNA-binding surface. Substitution of Phe by leucine in a ZFY peptide permits Zn(2+)-dependent folding. Although a native-like structure is retained, structural fluctuations lead to attenuation of selected nuclear Overhauser enhancements and accelerated amide proton exchange. Surprisingly, wild-type Zn affinity is maintained by entropy-enthalpy compensation (EEC): a hidden entropy penalty (TDeltaDeltaS 7kcal/mol) is balanced by enhanced enthalpy of association (DeltaDeltaH -7kcal/mol) at 25 degrees C. Because the variant is less well ordered than the Phe-anchored domain, the net change in entropy is opposite to the apparent change in configurational entropy. By analogy to the thermodynamics of organometallic complexation, we propose that EEC arises from differences in solvent reorganization. Exclusion of Leu among biological sequences suggests an evolutionary constraint on the dynamics of a Zn finger.
The hidden thermodynamics of a zinc finger.,Lachenmann MJ, Ladbury JE, Phillips NB, Narayana N, Qian X, Weiss MA J Mol Biol. 2002 Mar 1;316(4):969-89. PMID:11884136[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lachenmann MJ, Ladbury JE, Phillips NB, Narayana N, Qian X, Weiss MA. The hidden thermodynamics of a zinc finger. J Mol Biol. 2002 Mar 1;316(4):969-89. PMID:11884136 doi:10.1006/jmbi.2001.5335
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