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Structure, specificity, and mode of interaction for bacterial albumin-binding modules.

Johansson, Maria U ; Frick, Inga-Maria LU ; Nilsson, Hanna LU ; Kraulis, Per J ; Hober, Sophia ; Jonasson, Per ; Linhult, Martin ; Nygren, Per-Ake ; Uhlén, Mathias and Björck, Lars LU , et al. (2002) In Journal of Biological Chemistry 277(10). p.8114-8120
Abstract
We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns... (More)
We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Binding Competitive, Circular Dichroism, Dose-Response Relationship Drug, Drug Resistance, Evolution Molecular, Inhibitory Concentration 50, Kinetics, Magnetic Resonance Spectroscopy, Models Molecular, Molecular Sequence Data, Peptostreptococcus : metabolism, Protein Binding, Sequence Homology Amino Acid, Rabbits, Binding Sites, Amino Acid Sequence, Animal, Serum Albumin : chemistry : metabolism, Substrate Specificity, Support Non-U.S. Gov't, Temperature
in
Journal of Biological Chemistry
volume
277
issue
10
pages
8114 - 8120
publisher
ASBMB
external identifiers
  • wos:000174268000063
  • pmid:11751858
  • scopus:0037041036
  • pmid:11751858
ISSN
1083-351X
DOI
10.1074/jbc.M109943200
language
English
LU publication?
yes
id
013f28c0-7095-4514-ba0c-99681076d83b (old id 106969)
date added to LUP
2016-04-01 12:30:15
date last changed
2020-12-29 04:24:36
@article{013f28c0-7095-4514-ba0c-99681076d83b,
  abstract     = {We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.},
  author       = {Johansson, Maria U and Frick, Inga-Maria and Nilsson, Hanna and Kraulis, Per J and Hober, Sophia and Jonasson, Per and Linhult, Martin and Nygren, Per-Ake and Uhlén, Mathias and Björck, Lars and Drakenberg, Torbjörn and Forsén, Sture and Wikström, Mats},
  issn         = {1083-351X},
  language     = {eng},
  number       = {10},
  pages        = {8114--8120},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Structure, specificity, and mode of interaction for bacterial albumin-binding modules.},
  url          = {http://dx.doi.org/10.1074/jbc.M109943200},
  doi          = {10.1074/jbc.M109943200},
  volume       = {277},
  year         = {2002},
}