Campus Units
Chemistry
Document Type
Article
Publication Version
Published Version
Publication Date
10-16-1998
Journal or Book Title
Biochemistry
Volume
37
Issue
44
First Page
15423
Last Page
15433
DOI
10.1021/bi981773r
Abstract
Sequence analysis of surface proteins from Gram-positive bacteria indicates a composite organization consisting of unique and repeated segments. Thus, these proteins may contain discrete domains that could fold independently. In this paper, we have used a panel of biophysical methods, including gel permeation chromatography, analytical ultracentrifugation, circular dichroism, and fluorescence spectroscopy, to analyze the structural organization of the Staphylococcus aureus collagen adhesin, CNA. Our results indicate that the structure, function, and folding of the ligand-binding domain (A) are not affected by the presence or absence of the other major domain (B). In addition, little or no interaction is observed between the nearly identical repeat units within the B domain. We propose that CNA is indeed a mosaic protein in which the different domains previously indicated by sequence analysis operate independently.
Copyright Owner
American Chemical Society
Copyright Date
1998
Language
en
File Format
application/pdf
Recommended Citation
Rich, R. L.; Demeler, B.; Ashby, Kyle Donald; Deivanayagam, C. C.S.; Petrich, Jacob W.; Patti, J. M.; Narayana, S. V.L.; and Hook, M., "Domain Structure of the Staphylococcus aureus Collagen Adhesin" (1998). Chemistry Publications. 629.
https://lib.dr.iastate.edu/chem_pubs/629
Comments
Reprinted (adapted) with permission from Biochemistry 37 (1998): 15423, doi: 10.1021/bi981773r. Copyright 1998 American Chemical Society.