The GA module, a mobile albumin‐binding bacterial domain, adopts a three‐helix‐bundle structure

FEBS Letters

Drakenberg, Torbjörn²  Björck, Lars¹  Wikström, Mats²  de Château, Maarten¹  Johansson, Maria U.²  Forsén, Sture² 

[1] Department of Cell and Molecular Biology, Section for Molecular Pathogenesis, University of Lund, P.O.B 94, S-221 00 Lund, Sweden;Department of Physical Chemistry 2, Chemical Center, University of Lund, P.O.B 124, S-221 00 Lund, Sweden

关键词: Albumin binding;    Circular dichroism;    GA module;    NMR;    Protein PAB;    Three-helix bundle;    CD;    circular dichroism;    COSY;    J-correlated spectroscopy;    2Q;    double quantum;    GA;    protein G-related albumin-binding;    HSA;    human serum albumin;    Ig;    immunoglobulin;    NOE;    nuclear Overhauser effects;    NOESY;    nuclear Overhauser enhancement spectroscopy;    NMR;    nuclear magnetic resonance;    PAB;    peptostreptococcal albumin-binding;    PCR;    polymerase chain reaction;    R-COSY;    relayed COSY;    TOCSY;    total correlation spectroscopy;    T m;    transition midpoint of thermal denaturation;   

DOI  :  10.1016/0014-5793(95)01121-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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^αH 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.

【 授权许可】

Unknown