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PDBsum entry 1xeu
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Cell invasion
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PDB id
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1xeu
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References listed in PDB file
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Key reference
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Title
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Structure of internalin c from listeria monocytogenes.
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Authors
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A.Ooi,
S.Hussain,
A.Seyedarabi,
R.W.Pickersgill.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
1287-1293.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of internalin C (InlC) from Listeria monocytogenes has
been determined at 2.0 A resolution. Several observations implicate InlC in
infection: inlC has the same transcriptional activator as other virulence genes,
it is only present in pathogenic Listeria strains and an inlC deletion mutant is
significantly less virulent. While the extended concave receptor-binding
surfaces of the leucine-rich repeat (LRR) domains of internalins A and B have
aromatic clusters involved in receptor binding, the corresponding surface of
InlC is smaller, flatter and more hydrophilic, suggesting that InlC may be
involved in weak or transient associations with receptors; this may help explain
why no receptor has yet been discovered for InlC. In contrast, the Ig-like
domain, to which the LRR domain is fused, has surface aromatics that may be of
functional importance, possibly being involved in binding to the surface of the
bacteria or in receptor binding.
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Figure 1.
Figure 1 (a) Schematic drawing of the domain structure of
internalin C. (b) Electron density around Phe146, one of only
two exposed hydrophobic residues on the receptor-binding surface
of internalin C; also shown are adjacent leucine residues that
contribute to the hydrophobic core of the LRR domain. The 2.0
Å resolution  [A]-weighted
2F[obs] - F[calc] map was contoured at 1 .
(c) Stereo C^  trace
of the internalin C structure. (b) was prepared using BOBSCRIPT
(Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15,
132-134.]) and (c) and Fig. 4-(b) were prepared using PyMOL
(DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular
Visualization System. DeLano Scientific, San Carlos, CA, USA.
http://www.pymol.org .]).
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Figure 2.
Figure 2 (a) Structure of a typical LRR coil of internalin C,
comprising 22 residues. The LRR shown is coil four of six
present in InlC and corresponds to residues 141-162. The
hydrophobic core of the LRR domain is typically formed by
leucine residues at positions 2, 5, 7, 12, 15, 18 and 21. There
is an asparagine at position 10 in five out of the six turns;
the first turn is a variant and the first  -strand
of the Ig-like domain provides an equivalent glutamine. (b)
Structure of the unique 21-residue coil three of InlC (residues
120-140). The 3[10]-helix of the other coils (see a) is missing,
replaced by a 1-4
turn (residues 15-18) and a proline at position 19.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
1287-1293)
copyright 2006.
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