1zgk

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[[Image:1zgk.gif|left|200px]]
 
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==1.35 angstrom structure of the Kelch domain of Keap1==
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The line below this paragraph, containing "STRUCTURE_1zgk", creates the "Structure Box" on the page.
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<StructureSection load='1zgk' size='340' side='right'caption='[[1zgk]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zgk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZGK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1zgk| PDB=1zgk | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgk OCA], [https://pdbe.org/1zgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zgk RCSB], [https://www.ebi.ac.uk/pdbsum/1zgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zgk ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/1zgk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zgk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Kelch repeat is a common sequence motif in eukaryotic genomes and is approximately 50 amino acids in length. The structure of the Kelch domain of the human Keap1 protein has previously been determined at 1.85 Angstrom, showing that each Kelch repeat forms one blade of a six-bladed beta-propeller. Here, use of 1.35 Angstrom SAD data for de novo structure determination of the Kelch domain and for refinement at atomic resolution is described. The high quality and resolution of the diffraction data and phase information allows a detailed analysis of the role of solvent in the structure of the Kelch repeat. Ten structurally conserved water molecules are identified in each blade of the Kelch beta-propeller. These appear to play distinct structural roles that include lining the central channel of the propeller, interacting with residues in loops between strands of the blade and making contacts with conserved residues in the Kelch repeat. Furthermore, we identify a conserved C-H...pi hydrogen bond between two key residues in the consensus Kelch repeat. This analysis extends our understanding of the structural roles of conserved residues in the Kelch repeat and highlights the potential role of solvent in maintaining the fold of this common eukaryotic structural motif.
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'''1.35 angstrom structure of the Kelch domain of Keap1'''
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Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1.,Beamer LJ, Li X, Bottoms CA, Hannink M Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1335-42. Epub 2005, Sep 28. PMID:16204884<ref>PMID:16204884</ref>
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==Overview==
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The Kelch repeat is a common sequence motif in eukaryotic genomes and is approximately 50 amino acids in length. The structure of the Kelch domain of the human Keap1 protein has previously been determined at 1.85 Angstrom, showing that each Kelch repeat forms one blade of a six-bladed beta-propeller. Here, use of 1.35 Angstrom SAD data for de novo structure determination of the Kelch domain and for refinement at atomic resolution is described. The high quality and resolution of the diffraction data and phase information allows a detailed analysis of the role of solvent in the structure of the Kelch repeat. Ten structurally conserved water molecules are identified in each blade of the Kelch beta-propeller. These appear to play distinct structural roles that include lining the central channel of the propeller, interacting with residues in loops between strands of the blade and making contacts with conserved residues in the Kelch repeat. Furthermore, we identify a conserved C-H...pi hydrogen bond between two key residues in the consensus Kelch repeat. This analysis extends our understanding of the structural roles of conserved residues in the Kelch repeat and highlights the potential role of solvent in maintaining the fold of this common eukaryotic structural motif.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ZGK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGK OCA].
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</div>
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<div class="pdbe-citations 1zgk" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1., Beamer LJ, Li X, Bottoms CA, Hannink M, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1335-42. Epub 2005, Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204884 16204884]
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*[[Kelch-like protein 3D structures|Kelch-like protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beamer, L J.]]
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[[Category: Beamer LJ]]
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[[Category: Bottoms, C A.]]
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[[Category: Bottoms CA]]
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[[Category: Hannink, M.]]
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[[Category: Hannink M]]
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[[Category: Li, X.]]
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[[Category: Li X]]
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[[Category: Beta-propeller]]
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[[Category: Kelch repeat motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:35:50 2008''
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Current revision

1.35 angstrom structure of the Kelch domain of Keap1

PDB ID 1zgk

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