Premium
The GA module, a mobile albumin‐binding bacterial domain, adopts a three‐helix‐bundle structure
Author(s) -
Johansson Maria U.,
de Château Maarten,
Björck Lars,
Forsén Sture,
Drakenberg Torbjörn,
Wikström Mats
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01121-t
Subject(s) - circular dichroism , chemistry , protein secondary structure , helix bundle , crystallography , helix (gastropod) , albumin , nuclear magnetic resonance spectroscopy , protein structure , biophysics , stereochemistry , biochemistry , biology , ecology , snail
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 α 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.