PDBsum entry 4jeb

Electron transport

PDB id: 4jeb

Contents

Protein chains

106 a.a.

Ligands

HEM ×2

Metals

_ZN ×3

Waters ×39

PDB id:

4jeb

Name:

Electron transport

Title:

Crystal structure of an engineered ridc1 tetramer with four interfacial disulfide bonds and four three-coordinate zn(ii) sites

Structure:

Soluble cytochrome b562. Chain: a, b. Fragment: unp residues 23-128. Synonym: cytochrome b-562. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: cybc. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.30Å R-factor: 0.248 R-free: 0.309

Authors:

F.A.Tezcan,A.M.Medina-Morales,A.Perez,J.D.Brodin

Key ref:

A.Medina-Morales et al. (2013). In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds. J Am Chem Soc, 135, 12013-12022. PubMed id: 23905754 DOI: 10.1021/ja405318d

Date:

26-Feb-13 Release date: 21-Aug-13

Protein chains

P0ABE7  (C562_ECOLX) -  Soluble cytochrome b562 from Escherichia coli

Seq: 128 a.a.

Struc: 106 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1021/ja405318d

J Am Chem Soc 135:12013-12022 (2013)

PubMed id: 23905754

In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds.

A.Medina-Morales, A.Perez, J.D.Brodin, F.A.Tezcan.

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.