1JJW

Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution

Summary for 1JJW

• Entry DOI: 10.2210/pdb1jjw/pdb
• Related: 1G3K
• Descriptor: ATP-DEPENDENT PROTEASE HSLV, POTASSIUM ION (3 entities in total)
• Functional Keywords: k anomalous scattering, quasi-equivalent packing, hydrolase
• Biological source: Haemophilus influenzae
• Cellular location: Cytoplasm (By similarity): P43772
• Total number of polymer chains: 3
• Total formula weight: 56827.94

Authors

Sousa, M.C.,McKay, D.B. (deposition date: 2001-07-09, release date: 2001-12-05, Last modification date: 2023-08-16)

Primary citation

Sousa, M.C.,McKay, D.B.
Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
Acta Crystallogr.,Sect.D, 57:1950-1954, 2001

PubMed 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.

PubMed: 11717526
DOI: 10.1107/S090744490101575X

Experimental method

X-RAY DIFFRACTION (1.9 Å)