1kls

<StructureSection load='1kls' size='340' side='right'caption='[[1kls]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>

<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 [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" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5znf|5znf]], [[1klr|1klr]]</div></td></tr>

[[https://www.uniprot.org/uniprot/ZFY_HUMAN ZFY_HUMAN]] Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'.

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== 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<ref>PMID:11884136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kls" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lachenmann, M J]]

[[Category: Ladbury, J E]]

[[Category: Narayana, N]]

[[Category: Phillips, N B]]

[[Category: Qian, X]]

[[Category: Weiss, M A]]

[[Category: Zinc finger]]