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Title
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A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure.
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Author
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J.Wang.
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Ref.
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J Struct Biol, 2001,
134,
15-24.
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PubMed id
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Abstract
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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.
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