Characterization of monomeric and dimeric B domain of Staphylococcal protein A.
Both monomeric and dimeric constructs of the B domain of protein A from Staphylococcus aureus have been characterized by NMR, CD and fluorescence spectroscopy. The monomeric form of the protein was synthesized using a novel method incorporating the use of a recombinant, folded, chimeric protein. A comparison of the recombinant monomeric form with the commercially available dimeric form indicates that, although the dimer retains the integrity of the three-helix bundle structure present in the monomer, there are interdomain contacts in the dimeric form. A single long-lived water molecule in the hydrophobic core of the three-helix bundle of monomeric protein A may represent an important stabilizing factor for the three-helix bundle topology.
Karimi
A
A
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Matsumura
M
M
Wright
P E
PE
Dyson
H J
HJ
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019281:Dimerization; D005454:Fluorescence Polarization; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013205:Staphylococcal Protein A / Q000737:chemistry*
D011994:Recombinant Proteins; D013205:Staphylococcal Protein A