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[[Image:2bkg.gif|left|200px]]
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{{STRUCTURE_2bkg|  PDB=2bkg  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN'''


==Crystal structure of E3_19 a designed ankyrin repeat protein==
<StructureSection load='2bkg' size='340' side='right'caption='[[2bkg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/2bkg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2BKG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA].
</div>
<div class="pdbe-citations 2bkg" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Ankyrin 3D structures|Ankyrin 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Binz, H K.]]
<references/>
[[Category: Grutter, M G.]]
__TOC__
[[Category: Kohl, A.]]
</StructureSection>
[[Category: Pluckthun, A.]]
[[Category: Large Structures]]
[[Category: Ankyrin repeat]]
[[Category: Synthetic construct]]
[[Category: Consensus design]]
[[Category: Binz HK]]
[[Category: Designed protein]]
[[Category: Grutter MG]]
[[Category: Protein stability]]
[[Category: Kohl A]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:24:42 2008''
[[Category: Pluckthun A]]
Retrieved from "https://proteopedia.org/2bkg"