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PDBsum entry 1nm3
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Electron transport
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PDB id
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1nm3
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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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The tetrameric structure of haemophilus influenza hybrid prx5 reveals interactions between electron donor and acceptor proteins.
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Authors
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S.J.Kim,
J.R.Woo,
Y.S.Hwang,
D.G.Jeong,
D.H.Shin,
K.Kim,
S.E.Ryu.
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Ref.
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J Biol Chem, 2003,
278,
10790-10798.
[DOI no: ]
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PubMed id
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Abstract
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Cellular redox control is often mediated by oxidation and reduction of cysteine
residues in the redox-sensitive proteins, where thioredoxin and glutaredoxin
(Grx) play as electron donors for the oxidized proteins. Despite the importance
of protein-protein interactions between the electron donor and acceptor
proteins, there has been no structural information for the interaction of
thioredoxin or Grx with natural target proteins. Here, we present the crystal
structure of a novel Haemophilus influenza peroxiredoxin (Prx) hybrid Prx5
determined at 2.8-A resolution. The structure reveals that hybrid Prx5 forms a
tightly associated tetramer where active sites of Prx and Grx domains of
different monomers interact with each other. The Prx-Grx interface comprises
specific charge interactions surrounded by weak interactions, providing insight
into the target recognition mechanism of Grx. The tetrameric structure also
exhibits a flexible active site and alternative Prx-Grx interactions, which
appear to facilitate the electron transfer from Grx to Prx domain. Differences
of electron donor binding surfaces in Prx proteins revealed by an analysis based
on the structural information explain the electron donor specificities of
various Prx proteins.
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Figure 4.
Fig. 4. Environment of the redox active site. a, Prx-Grx
interaction and glutathione binding in the hyPrx5 tetramer.
Glutathione model (shown in the figure as a ball and stick
diagram) was created by superposing the complex structure of
Grx3-glutathione (PDB code 3GRX) on the hyPrx5 Grx domain.
Surfaces of Prx (monomer A) and Grx (monomer D) domains are
colored red and gold, respectively. Redox active cysteines
(Cys-49 and Cys-180) and residues involved in the Prx-Grx
interaction are labeled. b, stereo view of the 2F[o]  F[c]
electron density map. The electron density map around the Prx
active site of hyPrx5 is presented as superimposed with the
refined model. The map was contoured at a 0.9  level. c,
stereo view of the Prx active site of hyPrx5. The side chains of
residues (Arg-126 and Thr-46) contributing to the reactivity of
the sulfur atom of Cys-49 were drawn as a ball-and-stick
representation. Distances between the interacting atoms are
shown in the figure.
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Figure 5.
Fig. 5. Interaction surfaces implicated in the Prx-Grx or
Prx-Trx interaction. Electrostatic potential surfaces of the
hyPrx5 Prx domain, the hyPrx5 Grx domain, human Prx5 (PDB code
1HD2), and human Trx (PDB code 1ERU) were calculated by using
the program GRASP (27). Positive and negative charges are
represented as blue and red, respectively. a, the surface of the
hyPrx5 Prx domain. Residues involved in the Prx-Grx contact in
the hyPrx5 tetramer are labeled and surrounded by a yellow
lines. The alternative interaction surface (see "Prx-Grx
Interaction") is indicated with a green line. b, the surface of
the hyPrx5 Grx domain. Residues involved in the Prx-Grx contact
of in the hyPrx5 tetramer are labeled and surrounded by a yellow
line. c, the surface of human Prx5. Residues of human Prx5
corresponding to those participating in the Prx-Grx contact of
hyPrx5 are labeled and surrounded by a yellow line. The point of
view in the figure is the same as in a. The orientation was
determined by superposing the two structures (the hyPrx5 Prx
domain and human Prx5). Thr-48, Ser-51, Phe-150, Asp-154, and
Asp-156 of the hyPrx5 Prx domain correspond to Gly-46, Lys-49,
Leu-149, Leu-153, and Pro-155 of human Prx5, respectively (for
the sequence alignment, see Fig. 2). d, the surface of human
Trx. Residues of human Trx involved in the Trx-Trx reductase
contact (PDB code 1F6M) are labeled and surrounded by a yellow
line. The point of view in the figure is the same as in b. The
orientation was determined by superposing the two structures
(the hyPrx5 Grx domain and human Trx). The C  trace of
the NF  B peptide
bound to human Trx (Ref. 38, PDB code 1MDI) was drawn as a cyan
tube.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
10790-10798)
copyright 2003.
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