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PDBsum entry 3hte
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Motor protein
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PDB id
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3hte
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Contents |
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317 a.a.
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283 a.a.
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301 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Motor protein
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Title:
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Crystal structure of nucleotide-free hexameric clpx
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Structure:
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Atp-dependent clp protease atp-binding subunit clpx. Chain: a, b, c, d, e, f. Fragment: covalently linked clpx residues 62-424. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b0438, clpx, jw0428, lopc. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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4.03Å
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R-factor:
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0.279
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R-free:
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0.313
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Authors:
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S.E.Glynn,A.Martin,T.A.Baker,R.T.Sauer
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Key ref:
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S.E.Glynn
et al.
(2009).
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Cell,
139,
744-756.
PubMed id:
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Date:
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11-Jun-09
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Release date:
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24-Nov-09
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PROCHECK
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Headers
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References
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P0A6H1
(CLPX_ECOLI) -
ATP-dependent Clp protease ATP-binding subunit ClpX from Escherichia coli (strain K12)
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Seq:
Struc:
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424 a.a.
317 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.?
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Cell
139:744-756
(2009)
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PubMed id:
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Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
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S.E.Glynn,
A.Martin,
A.R.Nager,
T.A.Baker,
R.T.Sauer.
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ABSTRACT
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ClpX is a AAA+ machine that uses the energy of ATP binding and hydrolysis to
unfold native proteins and translocate unfolded polypeptides into the ClpP
peptidase. The crystal structures presented here reveal striking asymmetry in
ring hexamers of nucleotide-free and nucleotide-bound ClpX. Asymmetry arises
from large changes in rotation between the large and small AAA+ domains of
individual subunits. These differences prevent nucleotide binding to two
subunits, generate a staggered arrangement of ClpX subunits and pore loops
around the hexameric ring, and provide a mechanism for coupling conformational
changes caused by ATP binding or hydrolysis in one subunit to flexing motions of
the entire ring. Our structures explain numerous solution studies of ClpX
function, predict mechanisms for pore elasticity during translocation of
irregular polypeptides, and suggest how repetitive conformational changes might
be coupled to mechanical work during the ATPase cycle of ClpX and related
molecular machines.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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G.C.Lander,
E.Estrin,
M.E.Matyskiela,
C.Bashore,
E.Nogales,
and
A.Martin
(2012).
Complete subunit architecture of the proteasome regulatory particle.
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Nature,
482,
186-191.
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H.Schmidt,
E.S.Gleave,
and
A.P.Carter
(2012).
Insights into dynein motor domain function from a 3.3-Å crystal structure.
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Nat Struct Mol Biol,
19,
492.
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PDB codes:
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S.E.Glynn,
A.R.Nager,
T.A.Baker,
and
R.T.Sauer
(2012).
Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.
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Nat Struct Mol Biol,
19,
616-622.
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E.Gur,
D.Biran,
and
E.Z.Ron
(2011).
Regulated proteolysis in Gram-negative bacteria--how and when?
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Nat Rev Microbiol,
9,
839-848.
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F.Wang,
Z.Mei,
Y.Qi,
C.Yan,
Q.Hu,
J.Wang,
and
Y.Shi
(2011).
Structure and mechanism of the hexameric MecA-ClpC molecular machine.
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Nature,
471,
331-335.
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PDB codes:
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G.Tian,
S.Park,
M.J.Lee,
B.Huck,
F.McAllister,
C.P.Hill,
S.P.Gygi,
and
D.Finley
(2011).
An asymmetric interface between the regulatory and core particles of the proteasome.
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Nat Struct Mol Biol,
18,
1259-1267.
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M.Stotz,
O.Mueller-Cajar,
S.Ciniawsky,
P.Wendler,
F.U.Hartl,
A.Bracher,
and
M.Hayer-Hartl
(2011).
Structure of green-type Rubisco activase from tobacco.
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Nat Struct Mol Biol,
18,
1366-1370.
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PDB codes:
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O.Mueller-Cajar,
M.Stotz,
P.Wendler,
F.U.Hartl,
A.Bracher,
and
M.Hayer-Hartl
(2011).
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase.
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Nature,
479,
194-199.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
