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PDBsum entry 1g3k
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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 and solution structures of an hsluv protease-Chaperone complex.
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Authors
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M.C.Sousa,
C.B.Trame,
H.Tsuruta,
S.M.Wilbanks,
V.S.Reddy,
D.B.Mckay.
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Ref.
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Cell, 2000,
103,
633-643.
[DOI no: ]
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PubMed id
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Abstract
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HslUV is a "prokaryotic proteasome" composed of the HslV protease and
the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal
structure of an HslUV complex is presented here. Two hexameric ATP binding rings
of HslU bind intimately to opposite sides of the HslV protease; the HslU
"intermediate domains" extend outward from the complex. The solution
structure of HslUV, derived from small angle X-ray scattering data under
conditions where the complex is assembled and active, agrees with this
crystallographic structure. When the complex forms, the carboxy-terminal helices
of HslU distend and bind between subunits of HslV, and the apical helices of
HslV shift substantially, transmitting a conformational change to the active
site region of the protease.
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Figure 1.
Figure 1. Representative Electron Density MapsStereo views
of F[o] − F[c] simulated annealing omit maps, computed with
phases calculated from models in which the atoms of interest
were deleted from the model used in refinement.(A) the ATP
binding site of HslU, contoured at 5σ. Protein is shown as a
ribbon diagram; ATP from the final HslUV model (average B factor
29.3) is shown as a ball and stick representation.(B)
Carboxy-terminal segment of HslU (average B factor 119.1),
contoured at 3σ (magenta) and 6σ (cyan). Residues of HslU
which were omitted are shown in green, oriented with the
carboxy-terminal Leu-444 at the bottom of the figure;
neighboring residues of HslV are shown in standard colors
(oxygen, red; nitrogen, blue; carbon, gray). Figure was prepared
with BOBSCRIPT ([7 and 8]). The rendering and stereo pair
generation of all figures was done with RASTER3D ( [25]) and
IMAGEMAGIK
(http://www.wizards.dupont.com/cristy/ImageMagick.html).
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Figure 6.
Figure 6. Conformational Changes around the Catalytic Site
of HslVStereo ribbon drawing of the active site region. The
HslUV structure is colored green. The segment of uncomplexed
HslV that differs substantially from the complex (see Figure 3A)
is colored magenta. Selected residue side chains and polypeptide
backbone are shown in the ball and stick representation.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
103,
633-643)
copyright 2000.
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Added reference #1*
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Title
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Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
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Authors
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M.C.Sousa,
D.B.McKay.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1950-1954.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Quasi-equivalent subunit interactions within HslV. (a)
Ribbon drawing of one hexamer, looking down the pseudo-sixfold
axis. Subunits related by crystallographic twofold rotation are
shown in identical colors and denoted with a prime. Regions on
the apical helices which reveal differences in subunit-subunit
interactions are highlighted: magenta on cyan for subunit A; red
on yellow for subunit B; green on gold for subunit C. (b)
Interactions between subunits C and A, using same color coding
as in (a). (c) Interactions between subunits B and C. Figs.
1-and 2-(b) were produced with MOLSCRIPT (Kraulis, 1991[Kraulis,
P. (1991). J. Appl. Cryst. 24, 946-950.]) and Fig. 2-(a) was
produced with BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J.
Mol. Graph. 15, 132-134.], 1999[Esnouf, R. M. (1999). Acta
Cryst. D55, 938-940.]); all figures were rendered with Raster3D
(Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997).
Methods Enzymol. 277, 505-524.]).
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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*Note, "added" references are those not in the PDB file but
which have either been obtained from the journal or suggested by the
author(s).
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