4PLS

Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.

4PLS の概要

• エントリーDOI: 10.2210/pdb4pls/pdb
• 分子名称: Arm00010, CALCIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: peptide binding protein, designed armadillo repeat proteins, protein engineering
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118190.03

構造登録者

Reichen, C.,Madhurantakam, C.,Plueckthun, A.,Mittl, P.R. (登録日: 2014-05-19, 公開日: 2014-12-10, 最終更新日: 2023-12-20)

主引用文献

Reichen, C.,Madhurantakam, C.,Pluckthun, A.,Mittl, P.R.
Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.
Protein Sci., 23:1572-, 2014

PubMed Abstract: Designed armadillo repeat proteins (dArmRP) are promising modular proteins for the engineering of binding molecules that recognize extended polypeptide chains. We determined the structure of a dArmRP containing five internal repeats and 3rd generation capping repeats in three different states by X-ray crystallography: without N-terminal His6 -tag and in the presence of calcium (YM5 A/Ca(2+) ), without N-terminal His6 -tag and in the absence of calcium (YM5 A), and with N-terminal His6 -tag and in the presence of calcium (His-YM5 A/Ca(2+)). All structures show different quaternary structures and superhelical parameters. His-YM5 A/Ca(2+) forms a crystallographic dimer, which is bridged by the His6 -tag, YM5 A/Ca(2+) forms a domain-swapped tetramer, and only in the absence of calcium and the His6 -tag, YM5 A forms a monomer. The changes of superhelical parameters are a consequence of calcium binding, because calcium ions interact with negatively charged residues, which can also participate in the modulation of helix dipole moments between adjacent repeats. These observations are important for further optimizations of dArmRPs and provide a general illustration of how construct design and crystallization conditions can influence the exact structure of the investigated protein.

PubMed: 25132085
DOI: 10.1002/pro.2535

実験手法

X-RAY DIFFRACTION (2.35 Å)