Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Journal Article uri icon



  • The structure of the Haemophilus influenzae HslV protease of the HslUV 'prokaryotic proteasome' has been solved by molecular replacement and refined with data to 1.9 A resolution. The protease is a 'double donut' of hexameric rings; two alternative sets of intermolecular interactions between protomers in the rings result in 'quasi-equivalent' packing within the assembly. Anomalous scattering data from crystals with potassium present in the mother liquor reveal a K(+) ion bound with octahedral coordination near the active-site Thr1 residue. The site also binds Na(+) ions and is likely to bind Mg(2+), suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease.

publication date

  • December 1, 2001

has subject area

has restriction

  • closed

Date in CU Experts

  • October 18, 2013 3:36 AM

Full Author List

  • Sousa MC; McKay DB

author count

  • 2

Other Profiles

International Standard Serial Number (ISSN)

  • 0907-4449

Additional Document Info

start page

  • 1950

end page

  • 1954


  • 57


  • Pt 12