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PDBsum entry 1do0
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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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The structures of hsiu and the ATP-Dependent protease hsiu-Hsiv.
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Authors
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M.Bochtler,
C.Hartmann,
H.K.Song,
G.P.Bourenkov,
H.D.Bartunik,
R.Huber.
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Ref.
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Nature, 2000,
403,
800-805.
[DOI no: ]
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PubMed id
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Abstract
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The degradation of cytoplasmic proteins is an ATP-dependent process. Substrates
are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and
to a number of unrelated proteases in prokaryotes. A surprising link emerged
with the discovery of the ATP-dependent protease HslVU (heat shock locus VU) in
Escherichia coli. Its protease component HslV shares approximately 20% sequence
similarity and a conserved fold with 20S proteasome beta-subunits. HslU is a
member of the Hsp100 (Clp) family of ATPases. Here we report the crystal
structures of free HslU and an 820,000 relative molecular mass complex of HslU
and HslV-the first structure of a complete set of components of an ATP-dependent
protease. HslV and HslU display sixfold symmetry, ruling out mechanisms of
protease activation that require a symmetry mismatch between the two components.
Instead, there is conformational flexibility and domain motion in HslU and a
localized order-disorder transition in HslV. Individual subunits of HslU contain
two globular domains in relative orientations that correlate with nucleotide
bound and unbound states. They are surprisingly similar to their counterparts in
N-ethylmaleimide-sensitive fusion protein, the prototype of an AAA-ATPase. A
third, mostly alpha-helical domain in HslU mediates the contact with HslV and
may be the structural equivalent of the amino-terminal domains in proteasomal
AAA-ATPases.
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Figure 1.
Figure 1: Summary of the three crystal forms (a-c) that were
used for structure determination. Subunits in the respective
asymmetric units are numbered 1-6.
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Figure 2.
Figure 2: Comparison of HsIU and NSF main chains. a,
Superposition of the ligand-bound (coloured) and free (white)
HslU forms. Chains 1 and 2 of the P321 crystals (see Fig. 1c)
are shown. The N domains (shown in green and red) have been
superimposed (r.m.s.d. C  bond
lengths = 0.5 Å for the central  -sheet,
r.m.s.d. C bond
lengths = 1.2 Å for the whole domain). For clarity, the N and I
domains of the free form have been omitted. b, Stereo diagram of
NSF D2.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
403,
800-805)
copyright 2000.
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Secondary reference #1
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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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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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Secondary reference #2
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Title
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Hslv-Hslu: a novel ATP-Dependent protease complex in escherichia coli related to the eukaryotic proteasome.
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Authors
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M.Rohrwild,
O.Coux,
H.C.Huang,
R.P.Moerschell,
S.J.Yoo,
J.H.Seol,
C.H.Chung,
A.L.Goldberg.
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Ref.
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Proc Natl Acad Sci U S A, 1996,
93,
5808-5813.
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PubMed id
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Secondary reference #3
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Title
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Sequence analysis of four new heat-Shock genes constituting the hslts/ibpab and hslvu operons in escherichia coli.
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Authors
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S.E.Chuang,
V.Burland,
G.Plunkett,
D.L.Daniels,
F.R.Blattner.
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Ref.
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Gene, 1993,
134,
1-6.
[DOI no: ]
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PubMed id
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