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PDBsum entry 3emo
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Membrane protein/cell adhesion
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PDB id
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3emo
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References listed in PDB file
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Key reference
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Title
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Repetitive architecture of the haemophilus influenzae hia trimeric autotransporter.
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Authors
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G.Meng,
J.W.St geme,
G.Waksman.
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Ref.
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J Mol Biol, 2008,
384,
824-836.
[DOI no: ]
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PubMed id
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Abstract
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The Hia autotransporter of Haemophilus influenzae belongs to the trimeric
autotransporter subfamily and mediates bacterial adherence to the respiratory
epithelium. In this report, we show that the structure of Hia is characterized
by a modular architecture containing repeats of structurally distinct domains.
Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a
nonadhesive repeat (a novel fold) shed light on the structural determinants of
Hia adhesive function. Examination of the structure of an extended version of
the Hia translocator domain revealed the structural transition between the
C-terminal translocator domain and the N-terminal passenger domain, highlighting
a highly intertwined domain that is ubiquitous among trimeric autotransporters.
Overall, this study provides important insights into the mechanism of Hia
adhesive activity and the overall structure of trimeric autotransporters.
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Figure 4.
Fig. 4. Structure comparison between Trp-ring domains. (a)
Stereo ribbon diagram of the superimposed W1 (blue), W3 (green),
and W5 (red) domains viewed from the side. (b) Stereo ribbon
diagram of the superimposed Trp-ring domains viewed from the
top. (c) Sequence alignment of the Trp-ring domains between
Hia/Hsf/NhhA. In (a) and (b), the conserved residues at the
trimeric interface are shown in stick representation. In (c),
these residues are shown in blue.
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Figure 6.
Fig. 6. Modular architecture of Hia and putative two-step
adhesive mechanism. (a) Modular architecture of Hia adhesin.
While the structures of IN1, W1, KG1, W3, IN2, W5, Neck, and
transmembrane anchor/translocator domains are determined
crystallographically, W2/W4 and KG2 are modeled based on
W1/W3/W5 and KG1, respectively. Yellow rectangles represent the
Hia sequences that are yet to be structurally characterized,
including the predicted N-terminal GANG and C-terminal TTT
domains. (b) A putative two-step adhesive mechanism utilized by
Hia/Hsf-like adhesin to form an intimate association between the
bacterium and the host cell. The adhesive Trp-ring domains with
different binding capacities are shown in blue and red. The
nonadhesive Trp-ring domains are shown in green.
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The above figures are
reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2008,
384,
824-836)
copyright 2008.
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