A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure.
The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease. Crystal structures show that HslU forms a hexamer with a pore at one end and HslV forms a dodecamer with translocation pores at both ends of two back-to-back stacked hexameric rings. Consistent with three electron microscopic studies and one small-angle X-ray scattering study, three crystal structures show that the nucleotide-binding domains of HslU bind to HslV and that the pores of the peptidase and ATPase are next to each other and aligned. A fourth crystal structure shows a radically different quaternary arrangement. Here I present a crystallographic analysis of the fourth structure to show that it contained a crystallographic origin shift and a mistake in space group assignment. Once these errors are corrected, a quaternary arrangement that is similar to those observed in the other structures emerges.
Wang
J
J
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut 06520-8114, USA.
D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry; D008628:Mercury; D008958:Models, Molecular; D008968:Molecular Conformation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D012697:Serine Endopeptidases
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D000251:Adenosine Triphosphatases; D008628:Mercury