ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
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 Å 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 Mg2+, suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S090744490101575X
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