PDBsum entry 6ghh

Transport protein

PDB id: 6ghh

Contents

Protein chain

162 a.a.

Ligands

TDA

Waters ×79

PDB id:

6ghh

Name:

Transport protein

Title:

Thermodynamic, crystallographic and computational studies of non mammalian fatty acid binding to bovine b-lactoglobulin

Structure:

Beta-lactoglobulin. Chain: a. Synonym: beta-lg. Engineered: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Gene: lgb. Expressed in: bos taurus. Expression_system_taxid: 9913. Expression_system_tissue: milk

Resolution:

1.90Å R-factor: 0.199 R-free: 0.248

Authors:

G.Kontopidis,M.Rovoli

Key ref:

M.Rovoli et al. (2018). Thermodynamic, crystallographic and computational studies of non-mammalian fatty acid binding to bovine β-Lactoglobulin. Int J Biol Macromol, 118, 296-303. PubMed id: 29879410 DOI: 10.1016/j.ijbiomac.2018.05.226

Date:

07-May-18 Release date: 20-Jun-18

Protein chain

P02754  (LACB_BOVIN) -  Beta-lactoglobulin from Bos taurus

Seq: 178 a.a.

Struc: 162 a.a.

DOI no: 10.1016/j.ijbiomac.2018.05.226

Int J Biol Macromol 118:296-303 (2018)

PubMed id: 29879410

Thermodynamic, crystallographic and computational studies of non-mammalian fatty acid binding to bovine β-Lactoglobulin.

M.Rovoli, T.Thireou, Y.Choiset, T.Haertlé, L.Sawyer, E.Eliopoulos, G.Kontopidis.

ABSTRACT

The milk protein β-lactoglobulin has been widely studied since its discovery, both as a purified protein and in mixtures with other milk proteins, where its effect on the processing properties is of importance to the dairy industry. The protein can bind a variety of small hydrophobic molecules, which may allow its use as an oral delivery vehicle. In the present study we have examined the binding of odd-numbered fatty acids by isothermal calorimetry (ITC), X-ray crystallography and computer modelling to provide a clearer picture of the extent and variability of the central binding pocket. The Kd values for the fatty acids C13, C15, C16, C17 and C19 as determined by ITC are 1.93, 2.91, 3.05, 4.11 and 8.67 × 10^-7 M, respectively. The molecular structures revealed the ligands bound in the central cavity with generally well ordered lipophilic tails but significant positional variation at the carboxyl group end. In silico docking analyses identified the lipophilic interactions within the central cavity as the main driving force for binding with electrostatic interactions and H-bonds playing a minor role.