1jjw | pdb_00001jjw

Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution

spinqualitylabelsall models 1jjw, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jjw is a 3 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K Related: 1g3k Gene: HslV ("Bacterium influenzae" Lehmann and Neumann 1896) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HSLV_HAEIN] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.[HAMAP-Rule:MF_00248] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.,Sousa MC, McKay DB Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1950-4. Epub 2001, Nov 21. PMID:11717526 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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