PDBsum entry 5lyc

Oxidoreductase

PDB id: 5lyc

Contents

Protein chains

107 a.a.

Ligands

HEC ×2

7AZ ×2

SO4 ×5

Waters ×183

PDB id:

5lyc

Name:

Oxidoreductase

Title:

CytochromE C in complex with phosphonato-calix[6]arene

Structure:

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

Source:

Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: cyc1, yjr048w, j1653. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.170 R-free: 0.199

Authors:

M.L.Rennie,P.B.Crowley

Key ref:

M.L.Rennie et al. (2017). Protein Dimerization on a Phosphonated Calix[6]arene Disc. Angew Chem Int Ed Engl, 56, 5517-5521. PubMed id: 28407337 DOI: 10.1002/anie.201701500

Date:

27-Sep-16 Release date: 10-May-17

Protein chains

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

Seq: 109 a.a.

Struc: 107 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1002/anie.201701500

Angew Chem Int Ed Engl 56:5517-5521 (2017)

PubMed id: 28407337

Protein Dimerization on a Phosphonated Calix[6]arene Disc.

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

ABSTRACT

Complex formation between cationic cytochrome c and the water-soluble, poly-anionic p-phosphonatocalix[6]arene (pclx₆) was investigated. A crystal structure (at 1.8 Å resolution) revealed a remarkable dimeric disc of pclx₆that acts like glue to mediate a symmetric (C₂) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 Ųof protein surface. The key protein-calixarene contacts occur via two linchpin lysines, with additional contacts provided by a small hydrophobic patch. The protein-calixarene supramolecular assemblies were observed in solution by size-exclusion chromatography with multi-angle light scattering and NMR spectroscopy. Using isothermal titration calorimetry and NMR data, an apparent K_din the low micromolar range was determined for the charge-rich protein-calixarene complex. In contrast to p-sulfonatocalix[4]arene, the larger pclx₆has a single, well-defined binding site that mediates the assembly of cytochrome c in solution.