Volume 7 Issue 11, November 2000

Volume 7 Issue 11

Top view of the surface representation of the yeast proteasome core particle showing the peptide segments (dark blue) that regulate the entry into the active site chamber. These segments are at the C-termini of the seven distinct subunits forming the outer rings of the core particle. Note the near seven-fold symmetry of the top ring (illustrated by the yellow helices) and the breakdown of symmetry near the gating peptides. See pages 1062–1067, and News and Views pages 999–1001.


News & Views

  • News & Views |

    Escherichia coli cell division is restricted to the middle of the cell by the MinCDE system. Through complex interactions with MinC and MinD, the MinE protein promotes the correct placement of the cell division apparatus by specifically localizing to the cell center. The first detailed structural analysis of MinE provides key clues to help understand the critical actions of this protein.

    • Debrabrata RayChaudhuri
    • , G. Scott Gordon
    •  & Andrew Wright
  • News & Views |

    Two new crystal structures suggest that the eukaryotic proteasome is a gated protease and that opening of the gate may be a regulated event.

    • Cecile M. Pickart
    •  & Andrew P. VanDemark
  • News & Views |

    Two new crystal structures describe previously unresolved domains of the F1 sector of ATP synthase. These domains lie at the interface between the transmembrane rotary motor and the rotating subunits of the F1 domain and are crucial in coupling rotation of the two sectors to ATP synthesis.

    • Robert H. Fillingame

Picture Story


Review Article




  • Focus |

    Structural genomics

    Two sets of comprehensive reviews answer the questions of 'who? what? why? when? and how?' about the high-throughput, genome-wide structural analyses efforts across the globe.