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PDBsum entry 5ji2
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174 a.a.
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375 a.a.
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353 a.a.
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References listed in PDB file
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Key reference
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Title
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A structurally dynamic region of the hslu intermediate domain controls protein degradation and ATP hydrolysis.
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Authors
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V.Baytshtok,
X.Fei,
R.A.Grant,
T.A.Baker,
R.T.Sauer.
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Ref.
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Structure, 2016,
24,
1766-1777.
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PubMed id
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Abstract
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The I domain of HslU sits above the AAA+ ring and forms a funnel-like entry to
the axial pore, where protein substrates are engaged, unfolded, and translocated
into HslV for degradation. The L199Q I-domain substitution, which was originally
reported as a loss-of-function mutation, resides in a segment that appears to
adopt multiple conformations as electron density is not observed in HslU and
HslUV crystal structures. The L199Q sequence change does not alter the structure
of the AAA+ ring or its interactions with HslV but increases I-domain
susceptibility to limited endoproteolysis. Notably, the L199Q mutation increases
the rate of ATP hydrolysis substantially, results in slower degradation of some
proteins but faster degradation of other substrates, and markedly changes the
preference of HslUV for initiating degradation at the N or C terminus of model
substrates. Thus, a structurally dynamic region of the I domain plays a key role
in controlling protein degradation by HslUV.
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Secondary reference #1
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Title
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Crystal structures of the hslvu peptidase-Atpase complex reveal an ATP-Dependent proteolysis mechanism.
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Authors
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J.Wang,
J.J.Song,
M.C.Franklin,
S.Kamtekar,
Y.J.Im,
S.H.Rho,
I.S.Seong,
C.S.Lee,
C.H.Chung,
S.H.Eom.
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Ref.
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Structure, 2001,
9,
177-184.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. The Structures of HslVU(a) A composite-omit
electron density map (cyan, contoured at 1s) at 3.0 Å resolution
reveals that the bound dADP (yellow) is in an anti conformation,
not syn, as in a previously determined structure (AMPPNP,
magenta). This map was generated before dADP was built into the
model.(b) The HslVU complex in the asymmetric U[6]V[6]V[6]
configuration. Parts of HslU domain I could not be built into
the final electron density and are indicated by spheres for
their approximate locations.(c) The HslVU structure in the
symmetric U[6]V[6]V[6]U[6] configuration. The orientation of the
complexes in (1b) and (1c) differs by 30°
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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