The GA module, a mobile albumin-binding bacterial domain, adopts a three-helix-bundle structure.
We present the first study of the secondary structure and global fold of an albumin-binding domain. Our data show that the GA module from protein PAB, an albumin-binding protein from the anaerobic bacterial species Peptostreptococcus magnus, is composed of a left-handed three-helix bundle. The helical regions were identified by sequential and medium range NOEs, values of NH-C alpha H coupling constants, chemical shift indices, and the presence of slowly exchanging amide protons, as determined by NMR spectroscopy. In addition, circular dichroism studies show that the module is remarkably stable with respect to both pH and temperature.
Johansson
M U
MU
Department of Physical Chemistry 2, University of Lund, Sweden.
de Château
M
M
Björck
L
L
Forsén
S
S
Drakenberg
T
T
Wikström
M
M
D000418:Albumins / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002942:Circular Dichroism; D017931:DNA Primers; D004926:Escherichia coli; D006863:Hydrogen-Ion Concentration; D047908:Intracellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010462:Peptostreptococcus / Q000737:chemistry; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013696:Temperature
D000418:Albumins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D017931:DNA Primers; D047908:Intracellular Signaling Peptides and Proteins; D011994:Recombinant Proteins; C086961:PAB protein, Peptostreptococcus magnus