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PDBsum entry 1ned
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of heat shock locus V (hslv) from escherichia coli.
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Authors
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M.Bochtler,
L.Ditzel,
M.Groll,
R.Huber.
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Ref.
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Proc Natl Acad Sci U S A, 1997,
94,
6070-6074.
[DOI no: ]
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PubMed id
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Abstract
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Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the
ATP-dependent protease HslVU in Escherichia coli. It has sequence similarity
with the beta-type subunits of the eukaryotic and archaebacterial proteasomes.
Unlike these particles, which display 72-point symmetry, it is a dimer of
hexamers with 62-point symmetry. The crystal structure of HslV at 3.8-A
resolution, determined by isomorphous replacement and symmetry averaging, shows
that in spite of the different symmetry of the particle, the fold and the
contacts between subunits are conserved. A tripeptide aldehyde inhibitor,
acetyl-Leu-Leu-norleucinal, binds to the N-terminal threonine residue of HslV,
probably as a hemiacetal, relating HslV also functionally to the proteasomes of
archaea and eukaryotes.
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Figure 5.
Fig. 5. Overlay of HslV (red) with the T. acidophilum  -subunit
(green) with bound calpain inhibitors. The secondary structural
elements are labeled.
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Figure 6.
Fig. 6. Overlay of one hexameric ring of HslV (red) with one
heptameric ring of T. acidophilum -subunits
(green).
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