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2bkg

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[[Image:2bkg.gif|left|200px]]
 
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==Crystal structure of E3_19 a designed ankyrin repeat protein==
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The line below this paragraph, containing "STRUCTURE_2bkg", creates the "Structure Box" on the page.
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<StructureSection load='2bkg' size='340' side='right'caption='[[2bkg]], [[Resolution|resolution]] 1.90&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'>[[2bkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BKG 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]] 1.9&#8491;</td></tr>
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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=2bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkg OCA], [https://pdbe.org/2bkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bkg RCSB], [https://www.ebi.ac.uk/pdbsum/2bkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bkg ProSAT]</span></td></tr>
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{{STRUCTURE_2bkg| PDB=2bkg | SCENE= }}
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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/bk/2bkg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2bkg 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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Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.
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'''CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN'''
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Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability.,Binz HK, Kohl A, Pluckthun A, Grutter MG Proteins. 2006 Nov 1;65(2):280-4. PMID:16493627<ref>PMID:16493627</ref>
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==Overview==
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Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.
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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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2BKG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA].
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</div>
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<div class="pdbe-citations 2bkg" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability., Binz HK, Kohl A, Pluckthun A, Grutter MG, Proteins. 2006 Nov 1;65(2):280-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16493627 16493627]
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*[[Ankyrin 3D structures|Ankyrin 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Binz, H K.]]
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<references/>
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[[Category: Grutter, M G.]]
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__TOC__
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[[Category: Kohl, A.]]
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</StructureSection>
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[[Category: Pluckthun, A.]]
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[[Category: Large Structures]]
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[[Category: Ankyrin repeat]]
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[[Category: Synthetic construct]]
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[[Category: Consensus design]]
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[[Category: Binz HK]]
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[[Category: Designed protein]]
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[[Category: Grutter MG]]
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[[Category: Protein stability]]
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[[Category: Kohl A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:24:42 2008''
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[[Category: Pluckthun A]]

Current revision

Crystal structure of E3_19 a designed ankyrin repeat protein

PDB ID 2bkg

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