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| | ==Crystal structure of E3_19 a 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]] 1.90Å' scene=''> | + | <StructureSection load='2bkg' size='340' side='right'caption='[[2bkg]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BKG FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k1a|1k1a]], [[1k1b|1k1b]], [[1mj0|1mj0]], [[1n0q|1n0q]], [[1n0r|1n0r]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkg OCA], [http://pdbe.org/2bkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bkg RCSB], [http://www.ebi.ac.uk/pdbsum/2bkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bkg ProSAT]</span></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> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | ==See Also== | | ==See Also== |
| - | *[[Ankyrin|Ankyrin]] | + | *[[Ankyrin 3D structures|Ankyrin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Large Structures]] |
| - | [[Category: Binz, H K]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Grutter, M G]] | + | [[Category: Binz HK]] |
| - | [[Category: Kohl, A]] | + | [[Category: Grutter MG]] |
| - | [[Category: Pluckthun, A]] | + | [[Category: Kohl A]] |
| - | [[Category: Ankyrin repeat]]
| + | [[Category: Pluckthun A]] |
| - | [[Category: Consensus design]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Designed protein]]
| + | |
| - | [[Category: Protein stability]]
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| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Binz HK, Kohl A, Pluckthun A, Grutter MG. Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability. Proteins. 2006 Nov 1;65(2):280-4. PMID:16493627 doi:http://dx.doi.org/10.1002/prot.20930
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