Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
Acta Crystallogr D Biol Crystallogr
; 57(Pt 12): 1950-4, 2001 Dec.
Article
in En
| MEDLINE
| ID: mdl-11717526
ABSTRACT
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.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endopeptidases
/
Serine Endopeptidases
/
Haemophilus influenzae
/
Adenosine Triphosphatases
/
Heat-Shock Proteins
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
2001
Document type:
Article
Affiliation country:
Estados Unidos