Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C2221 . Structural differences between genetic variants A and B and features of the Tanford transition

Abstract

Abbreviations: BLG, b-lactoglobulin. Note: the co-ordinates for variants A and B of b-lactoglobulin lattice Y have been deposited in the RCSB Protein Data Bank with accession nos 1qg5 and 1b8e, respectively. q FEBS 2001 Structures of bovine b-lactoglobulin A and B (Eur. J. Biochem. 268) 479 q FEBS 2001 Structures of bovine b-lactoglobulin A and B (Eur. J. Biochem. 268) 481 q FEBS 2001 Structures of bovine b-lactoglobulin A and B (Eur. J. Biochem. 268) 483

Structural Plasticity and Enzyme Action: Crystal Structures of Mycobacterium tuberculosis Peptidyl-tRNA Hydrolase

“…Peptide binding is accompanied by the closure of a peptide stretch of the enzyme on the ligand, reminiscent of loop closure in other proteins such as, for example, GTP-binding proteins, 24 and β-lactoglobulin. 25,26 This closure leads to concerted movement of several residues, resulting in the opening of a channel connecting the peptide and the tRNA-binding sites. The residues involved in these movements, like those that take part in peptide and tRNA binding, are highly conserved in bacterial Pth, lending further support to the proposed model.…”

Structure of bovine β-lactoglobulin (variant A) at very low ionic strength

“…The ill-deWned GH loop is shown here as a helical turn. Table 2 Pairwise superposition of BLG monomers: entries correspond to numbers of atoms superimposing within a criterion of 0.5 Å a a Abbreviations and references: A-X BLGA lattice X, pH 6.5 (1beb) (Oliveira et al, 2001); A-Y BLGA lattice Y pH 7.9 (1qg5) (Oliveira et al, 2001); A-Z BLGA lattice Z pH 6.2 (3blg) (Qin et al, 1998a); A-UЈ BLGA lattice UЈ; A-YЈ BLGA lattice YЈ (Adams, 2003); A-Z BR BLGA lattice Z with 12-bromododecanoic acid bound (1bso) (Qin et al, 1998b); A-Z PA BLGA lattice Z with palmitate bound (1b0o) (Wu et al, 1999); B-Y BLGB lattice Y pH 7.9 (Oliveira et al, 2001); C-Y BLG variant C lattice Y (Bewley et al, 1997;G.B. Jameson, unpublished results).…”

“…Table 1 summarises the known crystal forms. Subsequent structure determinations have involved lattices X (triclinic) (Brownlow et al, 1997), Y (orthorhombic C222 1 ) (Bewley et al, 1997;Oliveira et al, 2001), and Z (trigonal P3 2 21) (Kontopidis et al, 2002;Qin et al, 1998a;Wu et al, 1999), due to the ease of reproducibility of the high ionic strength crystallisation conditions and the insensitivity of the crystallisation conditions to small variations.…”

Computational and experimental approaches assess the interactions between bovine β-lactoglobulin and synthetic compounds of pharmacological interest

“…Each monomer adopts a b-barrel fold, characterized by a central calyx with an internal hydrophobic surface. Its secondary structure consists of eight subsequent antiparallel b-strands, an a-helix and a short C-terminal b-strand [17][18][19][20][21]. At low pH, BLG is monomeric, with most structural features similar to the dimer [22][23][24][25].…”