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PDBsum entry 1k1c
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Transport protein
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PDB id
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1k1c
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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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Solution structure and dynamics of crh, The bacillus subtilis catabolite repression hpr.
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Authors
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A.Favier,
B.Brutscher,
M.Blackledge,
A.Galinier,
J.Deutscher,
F.Penin,
D.Marion.
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Ref.
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J Mol Biol, 2002,
317,
131-144.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure and dynamics of the Bacillus subtilis HPr-like protein,
Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence
identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier
protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system,
but contains no catalytic His15, the site of PEP-dependent phosphorylation in
HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is
known to be monomeric. Complete backbone and side-chain assignments were
obtained for the monomeric form, and 60 % of the dimer backbone resonances;
allowing the identification of the Crh dimer interface from chemical-shift
mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06)
A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer
structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but
has a few notable differences, including a change in the orientation of one of
the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal
strand with the beta4 strand. This shift results in a shortening of the surface
loop present in HPr and consequently provides a flatter surface in the region of
dimerisation contact, which may be related to the different oligomeric nature of
these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite
control protein A (CcpA) is proposed on the basis of highly conserved surface
side-chains between Crh and HPr. This binding site is consistent with the model
of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation
measured in the monomeric form also identified differential local mobility in
the helix B which is located in the vicinity of this site.
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Figure 7.
Figure 7. Comparison of binding surface for enzyme I and
enzyme IIA^Glc on E. coliHPr to the corresponding surface ofB.
subtilis HPr and Crh. The PDB entries used forE. coliHPr, B.
subtilis HPr and Crh are 1HDN,[31] 2HID [40] and 1K1C,
respectively. (a) The residues of helices A and B, involved in
analogous hydrophobic and/or electrostatic interactions in the
(HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes and
conserved inB. subtilis HPr are highlighted on the HPr surfaces.
The residues, whose side-chains participate in hydrophobic and
electrostatic interactions, are colored in green and blue,
respectively. The PTS active site residue His15 is indicated in
red and the CCR regulation site residue Ser46 in B. subtilis is
indicated in yellow. The corresponding residues of B. subtilis
Crh are colored in the same way but Gln15 of Crh is colored in
magenta. Leu50 of Crh, which is part of the central hydrophobic
core, is colored in dark green. (b) Stick representation of the
residues colored in (a). (c) Same picture as in (a) but
containing also residues situated around the hydrophobic core
involved in hydrophobic and/or electrostatic interactions in the
(HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes, but
which are only partly conserved in B. subtilis HPr and Crh.
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Figure 9.
Figure 9. Diagram showing the two proposed models for Crh
dimer topology. (a) direct association via the L1 and L2 loops.
(b) Association via the swapping of the b1 strand.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2002,
317,
131-144)
copyright 2002.
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Secondary reference #1
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Title
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Evidence for a dimerisation state of the bacillus subtilis catabolite repression hpr-Like protein, Crh.
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Authors
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F.Penin,
A.Favier,
R.Montserret,
B.Brutscher,
J.Deutscher,
D.Marion,
D.Galinier.
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Ref.
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J Mol Microbiol Biotechnol, 2001,
3,
429-432.
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PubMed id
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