8CH0

Crystal structure of an 8-repeat consensus TPR superhelix with Gadolinium.

8CH0 の概要

• エントリーDOI: 10.2210/pdb8ch0/pdb
• 分子名称: Consensus tetratricopeptide repeat protein, GADOLINIUM ATOM, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• 機能のキーワード: ctpr, polymorphism, metal coordination, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17384.93

構造登録者

Liutkus, M.,Rojas, A.L.,Cortajarena, A.L. (登録日: 2023-02-06, 公開日: 2024-02-21, 最終更新日: 2024-04-24)

主引用文献

Liutkus, M.,Sasselli, I.R.,Rojas, A.L.,Cortajarena, A.L.
Diverse crystalline protein scaffolds through metal-dependent polymorphism.
Protein Sci., 33:e4971-e4971, 2024

PubMed Abstract: As protein crystals are increasingly finding diverse applications as scaffolds, controlled crystal polymorphism presents a facile strategy to form crystalline assemblies with controllable porosity with minimal to no protein engineering. Polymorphs of consensus tetratricopeptide repeat proteins with varying porosity were obtained through co-crystallization with metal salts, exploiting the innate metal ion geometric requirements. A single structurally exposed negative amino acid cluster was responsible for metal coordination, despite the abundance of negatively charged residues. Density functional theory calculations showed that while most of the crystals were the most thermodynamically stable assemblies, some were kinetically trapped states. Thus, crystalline porosity diversity is achieved and controlled with metal coordination, opening a new scope in the application of proteins as biocompatible protein-metal-organic frameworks (POFs). In addition, metal-dependent polymorphic crystals allow direct comparison of metal coordination preferences.

PubMed: 38591647
DOI: 10.1002/pro.4971

実験手法

X-RAY DIFFRACTION (1.75 Å)