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.

Comments

Reprinted (adapted) with permission from Biochemistry 37 (1998): 15423, doi: 10.1021/bi981773r. Copyright 1998 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

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