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PDBsum entry 1p3h
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Contents |
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* Residue conservation analysis
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PDB id:
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Chaperone
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Title:
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Crystal structure of the mycobacterium tuberculosis chaperonin 10 tetradecamer
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Structure:
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10 kda chaperonin. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: protein cpn10, groes protein, bcg-a heat shock protein, 10 kda antigen. Engineered: yes
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Source:
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Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: gros or groes or mopb or cpn10 or rv3418c or mt3527 or mtcy78.11. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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40mer (from
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Resolution:
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2.80Å
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R-factor:
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0.259
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R-free:
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0.280
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Authors:
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M.M.Roberts,A.R.Coker,G.Fossati,P.Mascagni,A.R.M.Coates,S.P.Wood,Tb Structural Genomics Consortium (Tbsgc)
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Key ref:
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M.M.Roberts
et al.
(2003).
Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops.
J Bacteriol,
185,
4172-4185.
PubMed id:
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Date:
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17-Apr-03
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Release date:
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15-Jul-03
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Supersedes:
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PROCHECK
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Headers
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References
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P9WPE5
(CH10_MYCTU) -
Co-chaperonin GroES from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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100 a.a.
99 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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J Bacteriol
185:4172-4185
(2003)
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PubMed id:
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Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops.
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M.M.Roberts,
A.R.Coker,
G.Fossati,
P.Mascagni,
A.R.Coates,
S.P.Wood.
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ABSTRACT
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The crystal structure of Mycobacterium tuberculosis chaperonin 10 (cpn10(Mt))
has been determined to a resolution of 2.8 A. Two dome-shaped cpn10(Mt)
heptamers complex through loops at their bases to form a tetradecamer with 72
symmetry and a spherical cage-like structure. The hollow interior enclosed by
the tetradecamer is lined with hydrophilic residues and has dimensions of 30 A
perpendicular to and 60 A along the sevenfold axis. Tetradecameric cpn10(Mt) has
also been observed in solution by dynamic light scattering. Through its base
loop sequence cpn10(Mt) is known to be the agent in the bacterium responsible
for bone resorption and for the contribution towards its strong T-cell
immunogenicity. Superimposition of the cpn10(Mt) sequences 26 to 32 and 66 to 72
and E. coli GroES 25 to 31 associated with bone resorption activity shows them
to have similar conformations and structural features, suggesting that there may
be a common receptor for the bone resorption sequences. The base loops of cpn10s
in general also attach to the corresponding chaperonin 60 (cpn60) to enclose
unfolded protein and to facilitate its correct folding in vivo. Electron density
corresponding to a partially disordered protein subunit appears encapsulated
within the interior dome cavity of each heptamer. This suggests that the binding
of substrates to cpn10 is possible in the absence of cpn60.
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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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V.van Noort,
J.Seebacher,
S.Bader,
S.Mohammed,
I.Vonkova,
M.J.Betts,
S.Kühner,
R.Kumar,
T.Maier,
M.O'Flaherty,
V.Rybin,
A.Schmeisky,
E.Yus,
J.Stülke,
L.Serrano,
R.B.Russell,
A.J.Heck,
P.Bork,
and
A.C.Gavin
(2012).
Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
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Mol Syst Biol,
8,
571.
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C.Weiss,
A.Bonshtien,
O.Farchi-Pisanty,
A.Vitlin,
and
A.Azem
(2009).
Cpn20: Siamese twins of the chaperonin world.
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Plant Mol Biol,
69,
227-238.
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N.Numoto,
A.Kita,
and
K.Miki
(2005).
Crystal structure of the Co-chaperonin Cpn10 from Thermus thermophilus HB8.
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Proteins,
58,
498-500.
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PDB code:
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D.Pantazatos,
J.S.Kim,
H.E.Klock,
R.C.Stevens,
I.A.Wilson,
S.A.Lesley,
and
V.L.Woods
(2004).
Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.
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Proc Natl Acad Sci U S A,
101,
751-756.
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G.Fossati,
P.Cremonesi,
G.Izzo,
E.Rizzi,
G.Sandrone,
S.Harding,
N.Errington,
C.Walters,
B.Henderson,
M.M.Roberts,
A.R.Coates,
and
P.Mascagni
(2004).
The Mycobacterium tuberculosis chaperonin 10 monomer exhibits structural plasticity.
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Biopolymers,
75,
148-162.
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G.Fossati,
G.Izzo,
E.Rizzi,
E.Gancia,
D.Modena,
M.L.Moras,
N.Niccolai,
E.Giannozzi,
O.Spiga,
L.Bono,
P.Marone,
E.Leone,
F.Mangili,
S.Harding,
N.Errington,
C.Walters,
B.Henderson,
M.M.Roberts,
A.R.Coates,
B.Casetta,
and
P.Mascagni
(2003).
Mycobacterium tuberculosis chaperonin 10 is secreted in the macrophage phagosome: is secretion due to dissociation and adoption of a partially helical structure at the membrane?
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J Bacteriol,
185,
4256-4267.
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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
code is
shown on the right.
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Links
