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PDBsum entry 1dd4
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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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Flexibility, Conformational diversity and two dimerization modes in complexes of ribosomal protein l12.
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Authors
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M.C.Wahl,
G.P.Bourenkov,
H.D.Bartunik,
R.Huber.
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Ref.
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EMBO J, 2000,
19,
174-186.
[DOI no: ]
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PubMed id
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Abstract
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Protein L12, the only multicopy component of the ribosome, is presumed to be
involved in the binding of translation factors, stimulating factor-dependent GTP
hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved
in two space groups by the multiple anomalous dispersion method and refined at
2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises
two full-length L12 molecules and two N-terminal L12 fragments that are
associated in a specific, hetero-tetrameric complex with one
non-crystallographic 2-fold axis. The two full-length proteins form a tight,
symmetric, parallel dimer, mainly through their N-terminal domains. Each monomer
of this central dimer additionally associates in a different way with an
N-terminal L12 fragment. Both dimerization modes are unlike models proposed
previously and suggest that similar complexes may occur in vivo and in situ. The
structures also display different L12 monomer conformations, in accord with the
suggested dynamic role of the protein in the ribosomal translocation process.
The structures have been submitted to the Protein Databank
(http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4.
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Figure 4.
Figure 4 Electrostatic surface potential for the monomer (A),
dimer (B) and tetramer (C). A highly acidic surface is visible
in the oligomers. The monomer displays several hydrophobic
areas, especially in the N-terminal furrow, along the hinge
helix and on the underside of the CTD. These patches are
efficiently shielded from solvent in the oligomers. Regions used
for contacts a–d (Figure 3) are indicated. The figure was
produced with GRASP (Nicholls et al., 1991).
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Figure 8.
Figure 8 Wire diagram of the core L12 dimer (molecule coloring
as in Figure 3) with residues Glu11, Phe29 and Thr32 in space
filling mode and the molecular surface indicated as a glassy
envelope. The six residues emphasized, critical for the
interaction with r-protein L10, line the N-terminal furrows,
marking the path of the additional N-terminal fragments (green
and yellow). The figure was produced with DINO
(http://www.bioz.unibas.ch/~xray/di..).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2000,
19,
174-186)
copyright 2000.
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