1zgk

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[[Image:1zgk.gif|left|200px]]
 
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{{Structure
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==1.35 angstrom structure of the Kelch domain of Keap1==
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|PDB= 1zgk |SIZE=350|CAPTION= <scene name='initialview01'>1zgk</scene>, resolution 1.35&Aring;
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<StructureSection load='1zgk' size='340' side='right'caption='[[1zgk]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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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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|ACTIVITY=
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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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|GENE= KEAP1, KIAA0132 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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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}}
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1zgk" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Kelch-like protein 3D structures|Kelch-like protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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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__TOC__
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</StructureSection>
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==Reference==
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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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[[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 Thu Mar 20 15:35:11 2008''
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Current revision

1.35 angstrom structure of the Kelch domain of Keap1

PDB ID 1zgk

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