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Volume 15 Issue 2, February 2008

Unfolding and degradation of protein substrates containing the ssrA tag by the bacterial AAA+ ClpXP is shown by Sauer and colleagues to be dependent on the rate of ATP hydrolysis and the substrate's energy landscape. Unfolding is represented by origami in the cover photograph by Erin Boyle. Origami by Adam Lipkin.pp 139-145

Volume 15 Issue 2

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Editorial

  • Metagenomics has the potential to shed light on one of the least understood group of organisms on Earth, while also providing useful tools for many fields in biology.

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Correspondence

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Meeting Report

  • Structural biology is making significant contributions toward an understanding of molecular constituents and mechanisms underlying human diseases at an atomic resolution, as discussed at the international Murnau Conference on Structural Biology of Disease Mechanisms held in September 2007 in Murnau, Germany.

    • K Ulrich Wendt
    • Manfred S Weiss
    • Dirk W Heinz
    Meeting Report
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News & Views

  • An immense range of polysaccharide structures is expressed on the bacterial surface. The length of the polymer can be a crucial attribute for virulence. Members of a family of 'polysaccharide copolymerase' proteins are essential for the regulation of polymer chain length, participating in one widespread biosynthesis scheme.

    • Chris Whitfield
    • Kane Larue
    News & Views

  • Recent papers shed insight into the architecture and dynamics of the components of the bacterial replisome.

    • Kenneth J Marians
    News & Views

  • Bacterial type III secretion machines have adapted to carry out numerous functions, ranging from locomotion to protein delivery into nucleated cells. One of the most intriguing issues is the source of energy that fuels their activities. Despite recent advances, there are still many questions to be resolved.

    • Jorge E. Galán
    News & Views
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