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PDBsum entry 1p9h
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Cell adhesion
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PDB id
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1p9h
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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 yersinia adhesin yada collagen-Binding domain structure is a novel left-Handed parallel beta-Roll.
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Authors
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H.Nummelin,
M.C.Merckel,
J.C.Leo,
H.Lankinen,
M.Skurnik,
A.Goldman.
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Ref.
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EMBO J, 2004,
23,
701-711.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the recombinant collagen-binding domain of Yersinia
adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 A
resolution. The trimeric structure is composed of head and neck regions, and the
collagen binding head region is a novel nine-coiled left-handed parallel
beta-roll. Before the beta-roll, the polypeptide loops from one monomer to the
rest, and after the beta-roll the neck region does the same, making the
transition from the globular head region to the narrower stalk domain. This
creates an intrinsically stable 'lock nut' structure. The trimeric form of YadA
is required for collagen binding, and mutagenesis of its surface residues
allowed identification of a putative collagen-binding surface. Furthermore, a
new structure-sequence motif for YadA beta-roll was used to identify putative
YadA-head-like domains in a variety of human and plant pathogens. Such domains
may therefore be a common bacterial strategy for avoiding host response.
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Figure 4.
Figure 4 (A) Organisation of the neck region in the C-terminus
of the head domain, viewed from the C-terminus along the z-axis.
The safety-pin structures as well as the beginnings of the stalk
domain helices are shown. Some residues in the neck region are
numbered for the magenta monomer for clarity. (B) The neck
region (viewed perpendicular to (A) showing one multi-centre
ionic network in the safety-pin region. It ties the three
'safety pins' to the central  -roll
assembly. The colouring of the monomers is the same as in Figure
1C.
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Figure 5.
Figure 5 Most likely orientation of the collagen triple helix on
the surface of the trimeric YadA head domain. The mutant
residues are coloured according to their effect on type I
collagen so that the mutants that abolished the binding totally
are coloured red, to <20% in orange and the ones that attenuated
the binding in violet. The residues D180 and E182, which also
had an effect on the trimeric structure, are in blue. The figure
was prepared using PyMOL (DeLano, 2002).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
701-711)
copyright 2004.
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