2bkg
From Proteopedia
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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: ]]
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