2BKG

Crystal structure of E3_19 a designed ankyrin repeat protein

2BKG の概要

• エントリーDOI: 10.2210/pdb2bkg/pdb
• 関連するPDBエントリー: 1K1A 1K1B 1MJ0 1N0Q 1N0R
• 分子名称: SYNTHETIC CONSTRUCT ANKYRIN REPEAT PROTEIN E3_19 (2 entities in total)
• 機能のキーワード: designed protein, ankyrin repeat, consensus design, protein stability, de novo protein
• 由来する生物種: SYNTHETIC CONSTRUCT
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35605.62

構造登録者

Binz, H.K.,Kohl, A.,Pluckthun, A.,Grutter, M.G. (登録日: 2005-02-16, 公開日: 2006-06-21, 最終更新日: 2024-01-31)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)