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PDBsum entry 2pr0
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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 sylvaticin, A new alpha-Elicitin-Like protein from pythium sylvaticum.
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Authors
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M.B.Lascombe,
P.Retailleau,
M.Ponchet,
B.Industri,
J.P.Blein,
T.Prangé.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2007,
63,
1102-1108.
[DOI no: ]
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PubMed id
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Abstract
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The structure of sylvaticin, a 10 kDa major pythin protein excreted by the
parasitic oomycete Pythium sylvaticum, has been determined. Although closely
related to alpha-elicitins in its biological response, toxicity and overall
structure, sylvaticin presents a number of structural features that make it an
unusual member of the elicitin class. Elicitins possess a large hydrophobic
cavity and the mechanism of the systemic acquired resistance induced in planta
is known to proceed through lipid transport and complexation within this cavity.
Unlike other elicitins, sylvaticin contains tryptophan residues, one of which
points inwards towards the central cavity, thus limiting access to sterols. In
the case of sylvaticin, the sterol-transport mechanism is likely to be of less
importance compared with other members of the elicitin family and still remains
to be fully characterized.
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Figure 3.
Figure 3 Two orthogonal views of ribbon diagrams of the
three-dimensional structure of sylvaticin, showing the
head-to-tail dimerization of sylvaticin around the two nickel
cations (green spheres) in the monoclinic form (the
metal-mediated dimer). The same arrangement is also observed in
the triclinic crystals.
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Figure 5.
Figure 5 The hydrophobic interface between two adjacent
sylvaticin dimers (the hydrophobic dimer). The packing contacts
between the two neighbours involve eight phenylalanine side
chains (Phe9, Phe12, Phe13, Phe75 and their symmetry-related
mates).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
1102-1108)
copyright 2007.
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Secondary reference #1
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Title
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Purification, Crystallization and preliminary X-Ray studies of sylvaticin, An elicitin-Like protein from pythium sylvaticum.
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Authors
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M.B.Lascombe,
M.Ponchet,
L.Cardin,
M.L.Milat,
J.P.Blein,
T.Prangé.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
362-364.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Sylvaticin crystals.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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