Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/266373
- author
- Lejon, S ; Frick, Inga-Maria LU ; Björck, Lars LU ; Wikstrom, M and Svensson, S
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 279
- issue
- 41
- pages
- 42924 - 42928
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000224226400071
- scopus:5644272668
- pmid:15269208
- 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
- 2016-04-01 11:55:41
- date last changed
- 2022-04-20 23:52:44
@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 = {{American Society for Biochemistry and Molecular Biology}}, 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}}, doi = {{10.1074/jbc.M406957200}}, volume = {{279}}, year = {{2004}}, }