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Title: Structure of a mutant [beta] toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility

Abstract

The 3.35 {angstrom} resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase {beta} toxin in which a conserved hydrophobic {beta}-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal {beta}-strand, leading to the formation of dimers linked by a conformationally flexible hinge region. Eight dimers are seen in the asymmetric unit, exhibiting a broad spectrum of conformations trapped in place by intermolecular contacts within the crystal lattice. Furthermore, the 16 monomers within each asymmetric unit exhibit a remarkable heterogeneity in thermal factors, which can be accounted for by the varying degrees to which each monomer interacts with other molecules in the crystal. This structure provides a unique example of the challenges associated with crystallographic study of flexible proteins.

Authors:
; ; ; ; ;  [1]
  1. (UMM)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
UNIVERSITY
OSTI Identifier:
1021791
Resource Type:
Journal Article
Journal Name:
Acta Crystallogr. F
Additional Journal Information:
Journal Volume: 67; Journal Issue: (4) ; 04, 2011; Journal ID: ISSN 1744-3091
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CRYSTAL LATTICES; CRYSTAL STRUCTURE; DIMERS; FLEXIBILITY; MONOMERS; MUTANTS; MUTATIONS; PROTEINS; RESOLUTION; STAPHYLOCOCCUS; TOXINS

Citation Formats

Kruse, Andrew C., Huseby, Medora J., Shi, Ke, Digre, Jeff, Ohlendorf, Douglas H., and Earhart, Cathleen A. Structure of a mutant [beta] toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility. United States: N. p., 2011. Web. doi:10.1107/S1744309111005239.
Kruse, Andrew C., Huseby, Medora J., Shi, Ke, Digre, Jeff, Ohlendorf, Douglas H., & Earhart, Cathleen A. Structure of a mutant [beta] toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility. United States. doi:10.1107/S1744309111005239.
Kruse, Andrew C., Huseby, Medora J., Shi, Ke, Digre, Jeff, Ohlendorf, Douglas H., and Earhart, Cathleen A. Fri . "Structure of a mutant [beta] toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility". United States. doi:10.1107/S1744309111005239.
@article{osti_1021791,
title = {Structure of a mutant [beta] toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility},
author = {Kruse, Andrew C. and Huseby, Medora J. and Shi, Ke and Digre, Jeff and Ohlendorf, Douglas H. and Earhart, Cathleen A.},
abstractNote = {The 3.35 {angstrom} resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase {beta} toxin in which a conserved hydrophobic {beta}-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal {beta}-strand, leading to the formation of dimers linked by a conformationally flexible hinge region. Eight dimers are seen in the asymmetric unit, exhibiting a broad spectrum of conformations trapped in place by intermolecular contacts within the crystal lattice. Furthermore, the 16 monomers within each asymmetric unit exhibit a remarkable heterogeneity in thermal factors, which can be accounted for by the varying degrees to which each monomer interacts with other molecules in the crystal. This structure provides a unique example of the challenges associated with crystallographic study of flexible proteins.},
doi = {10.1107/S1744309111005239},
journal = {Acta Crystallogr. F},
issn = {1744-3091},
number = (4) ; 04, 2011,
volume = 67,
place = {United States},
year = {2011},
month = {9}
}