8CH0

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

Summary for 8CH0

• Entry DOI: 10.2210/pdb8ch0/pdb
• Descriptor: Consensus tetratricopeptide repeat protein, GADOLINIUM ATOM, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: ctpr, polymorphism, metal coordination, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 17384.93

Authors

Liutkus, M.,Rojas, A.L.,Cortajarena, A.L. (deposition date: 2023-02-06, release date: 2024-02-21, Last modification date: 2024-04-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)