2BKG

Crystal structure of E3_19 a designed ankyrin repeat protein

Summary for 2BKG

• Entry DOI: 10.2210/pdb2bkg/pdb
• Related: 1K1A 1K1B 1MJ0 1N0Q 1N0R
• Descriptor: SYNTHETIC CONSTRUCT ANKYRIN REPEAT PROTEIN E3_19 (2 entities in total)
• Functional Keywords: designed protein, ankyrin repeat, consensus design, protein stability, de novo protein
• Biological source: SYNTHETIC CONSTRUCT
• Total number of polymer chains: 2
• Total formula weight: 35605.62

Authors

Binz, H.K.,Kohl, A.,Pluckthun, A.,Grutter, M.G. (deposition date: 2005-02-16, release date: 2006-06-21, Last modification date: 2024-01-31)

Primary citation

Binz, H.K.,Kohl, A.,Pluckthun, A.,Grutter, M.G.
Crystal Structure of a Consensus-Designed Ankyrin Repeat Protein: Implications for Stability
Proteins: Struct., Funct., Bioinf., 65:280-, 2006

PubMed Abstract: 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.

PubMed: 16493627
DOI: 10.1002/PROT.20930

Experimental method

X-RAY DIFFRACTION (1.9 Å)