2bkg
From Proteopedia
(New page: 200px<br /><applet load="2bkg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bkg, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
| - | Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very | + | 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== | ==About this Structure== | ||
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[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Binz, H | + | [[Category: Binz, H K.]] |
| - | [[Category: Grutter, M | + | [[Category: Grutter, M G.]] |
[[Category: Kohl, A.]] | [[Category: Kohl, A.]] | ||
[[Category: Pluckthun, A.]] | [[Category: Pluckthun, A.]] | ||
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[[Category: protein stability]] | [[Category: protein stability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:44 2008'' |
Revision as of 14:38, 21 February 2008
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CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN
Overview
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
2BKG is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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 [[Category: ]]
Page seeded by OCA on Thu Feb 21 16:38:44 2008
