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Crystal structure of a bacterial albumin‐binding domain at 1.4 Å resolution
Author(s) -
Cramer Jacob Flyvholm,
Nordberg Peter A.,
Hajdu Janos,
Lejon Sara
Publication year - 2007
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/j.febslet.2007.06.003
Subject(s) - albumin , crystal structure , plasma protein binding , protein structure , chemistry , serum albumin , crystallography , protein crystallization , binding domain , biophysics , biochemistry , biology , binding site , crystallization , organic chemistry
The albumin‐binding domain, or GA module, of the peptostreptococcal albumin‐binding protein expressed in pathogenic strains of Finegoldia magna is believed to be responsible for the virulence and increased growth rate of these strains. Here we present the 1.4 Å crystal structure of this domain, and compare it with the crystal structure of the GA–albumin complex. An analysis of protein–protein interactions in the two crystals, and the presence of multimeric GA species in solution, indicate the GA module is “sticky”, and is capable of forming contacts with a range of protein surfaces. This might lead to interactions with different host proteins.