4JEA

Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide bonds

Summary for 4JEA

• Entry DOI: 10.2210/pdb4jea/pdb
• Related: 2BC5 2QLA 3HNI 3HNK 3IQ5 3IQ6 4JE9 4JEB
• Descriptor: soluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (5 entities in total)
• Functional Keywords: four-helix bundle, electron transport
• Biological source: Escherichia coli
• Cellular location: Periplasm: P0ABE7
• Total number of polymer chains: 4
• Total formula weight: 50100.63

Authors

Tezcan, F.A.,Medina-Morales, A.M.,Perez, A.,Brodin, J.D. (deposition date: 2013-02-26, release date: 2013-08-21, Last modification date: 2024-10-16)

Primary citation

Medina-Morales, A.,Perez, A.,Brodin, J.D.,Tezcan, F.A.
In Vitro and Cellular Self-Assembly of a Zn-Binding Protein Cryptand via Templated Disulfide Bonds.
J.Am.Chem.Soc., 135:12013-12022, 2013

PubMed Abstract: Simultaneously strong and reversible through redox chemistry, disulfide bonds play a unique and often irreplaceable role in the formation of biological and synthetic assemblies. In an approach inspired by supramolecular chemistry, we report here that engineered noncovalent interactions on the surface of a monomeric protein can template its assembly into a unique cryptand-like protein complex ((C81/C96)RIDC14) by guiding the selective formation of multiple disulfide bonds across different interfaces. Owing to its highly interconnected framework, (C81/C96)RIDC14 is well preorganized for metal coordination in its interior, can support a large internal cavity surrounding the metal sites, and can withstand significant alterations in inner-sphere metal coordination. (C81/C96)RIDC14 self-assembles with high fidelity and yield in the periplasmic space of E. coli cells, where it can successfully compete for Zn(II) binding.

PubMed: 23905754
DOI: 10.1021/ja405318d

Experimental method

X-RAY DIFFRACTION (1.22 Å)