PDBsum entry 5kpf

Electron transport

PDB id: 5kpf

Contents

Protein chains

108 a.a.

Ligands

HEC ×2

NO3

6VJ

Waters ×265

PDB id:

5kpf

Name:

Electron transport

Title:

Crystal structure of cytochromE C - phenyl-trisulfonatocalix[4]arene complex

Structure:

CytochromE C iso-1. Chain: a, b. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: cyc1, yjr048w, j1653. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.70Å R-factor: 0.160 R-free: 0.207

Authors:

A.M.Doolan,M.L.Rennie,P.B.Crowley

Key ref:

A.M.Doolan et al. (2018). Protein Recognition by Functionalized Sulfonatocalix[4]arenes. Chemistry, 24, 984-991. PubMed id: 29125201 DOI: 10.1002/chem.201704931

Date:

04-Jul-16 Release date: 12-Jul-17

Protein chains

P00044  (CYC1_YEAST) -  Cytochrome c isoform 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 109 a.a.

Struc: 108 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1002/chem.201704931

Chemistry 24:984-991 (2018)

PubMed id: 29125201

Protein Recognition by Functionalized Sulfonatocalix[4]arenes.

A.M.Doolan, M.L.Rennie, P.B.Crowley.

ABSTRACT

The interactions of two mono-functionalized sulfonatocalix[4]arenes with cytochrome c were investigated by structural and thermodynamic methods. The replacement of a single sulfonate with either a bromo or a phenyl substituent resulted in altered recognition of cytochrome c as evidenced by X-ray crystallography. The bromo-substituted ligand yielded a new binding mode in which a self-encapsulated calixarene dimer contributed to crystal packing. This ligand also formed a weak halogen bond with the protein. The phenyl-substituted ligand was bound to Lys4 of cytochrome c, in a 1.7 Å resolution crystal structure. A dimeric packing arrangement mediated by ligand-ligand contacts in the crystal suggested a possible assembly mechanism. The different protein recognition properties of these calixarenes are discussed.