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Transcript
Biochimica et Biophysica Acta 1778 (2008) 1697
Contents lists available at ScienceDirect
Biochimica et Biophysica Acta
j o u r n a l h o m e p a g e : w w w. e l s ev i e r. c o m / l o c a t e / b b a m e m
Preface
Structural proteomics of the cell envelope of Gram-negative bacteria
The cell envelope of Gram-negative bacteria, including the plasma
membrane, the periplasmic space, and the outer membrane, can be
viewed as a model organelle with a large number of diverse critical
functions for bacterial physiology. A significant number of protein
structures of both the inner and outer membrane, as well as proteins
from the periplasm, have been solved by NMR or X-ray at an
increasing rate over the past few years. Proteomics techniques have
begun to make it possible to obtain a detailed inventory of the
contents of the cell envelope of Gram-negative bacteria. The methods
and data are now maturing to provide information about the
interactions between the different proteins and other biomolecules.
Biochemical and biophysical approaches have given a great deal of
information about the cellular processes occurring in the envelope,
including bioenergetics, transport, signaling, cell wall synthesis, and
various other catalytic activities.
The contributions in this special issue provide a timely review of
major aspects of the envelope components with known structures and
their environment. They complement the more microbiological
approach in a recent book [1]. The degree of detail in our current
understanding of the cell envelope and its processes suggests the cell
envelope may become one of the first organelles that is sufficiently
studied and understood to create computational models with
predictive powers at a cellular level.
Several reviews focus on individual classes of proteins, e.g.,
mechanosensitive channels and ABC transporters; others focus on
0005-2736/$ – see front matter © 2008 Elsevier B.V. All rights reserved.
doi:10.1016/j.bbamem.2008.08.008
functional systems, such as the iron import cascade, protein
secretion systems and the flagellar assembly; while yet others
review the state of the art in methodological developments in
crystallography, proteomics, and computational investigations in
membrane proteins.
We thank the authors of all contributions for their efforts.
Reference
[1] M. Ehrmann (Ed.), The Periplasm, American Society Microbiology, 2007.
D. Peter Tieleman⁎
Raymond J. Turner
Hans J. Vogel
Department of Biological Sciences, University of Calgary,
Calgary AB T2N1N4, Canada
E-mail addresses: tieleman@ucalgary (D.P. Tieleman),
[email protected] (R.J. Turner),
[email protected] (H.J. Vogel).
⁎Corresponding author.
Joel H. Weiner
Department of Biochemistry, University of Alberta, Alberta, Canada
E-mail address: [email protected] (J.H. Weiner).