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Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin

Lejon, S; Frick, Inga-Maria LU ; Björck, Lars LU ; Wikstrom, M and Svensson, S (2004) In Journal of Biological Chemistry 279(41). p.42924-42928
Abstract
Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna ( formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 Angstrom and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were... (More)
Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna ( formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 Angstrom and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were found to be involved in HSA binding. Furthermore, the presence of HSA-bound fatty acids seems to influence HSA-GA complex formation. F. magna has a much more restricted host specificity compared with C and G streptococci, which is also reflected in the binding of different animal albumins by proteins PAB and G. The structure of the HSA-GA complex offers a molecular explanation to this unusually clear example of bacterial adaptation. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
279
issue
41
pages
42924 - 42928
publisher
ASBMB
external identifiers
  • wos:000224226400071
  • scopus:5644272668
ISSN
1083-351X
DOI
10.1074/jbc.M406957200
language
English
LU publication?
yes
id
edccc26b-80d8-4027-a195-501df17fcd5b (old id 266373)
date added to LUP
2007-10-24 12:13:13
date last changed
2017-11-05 03:35:13
@article{edccc26b-80d8-4027-a195-501df17fcd5b,
  abstract     = {Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna ( formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 Angstrom and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were found to be involved in HSA binding. Furthermore, the presence of HSA-bound fatty acids seems to influence HSA-GA complex formation. F. magna has a much more restricted host specificity compared with C and G streptococci, which is also reflected in the binding of different animal albumins by proteins PAB and G. The structure of the HSA-GA complex offers a molecular explanation to this unusually clear example of bacterial adaptation.},
  author       = {Lejon, S and Frick, Inga-Maria and Björck, Lars and Wikstrom, M and Svensson, S},
  issn         = {1083-351X},
  language     = {eng},
  number       = {41},
  pages        = {42924--42928},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin},
  url          = {http://dx.doi.org/10.1074/jbc.M406957200},
  volume       = {279},
  year         = {2004},
}