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PDBsum entry 2d5f
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Plant protein
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PDB id
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2d5f
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References listed in PDB file
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Key reference
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Title
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Conservation and divergence on plant seed 11s globulins based on crystal structures.
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Authors
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M.R.Tandang-Silvas,
T.Fukuda,
C.Fukuda,
K.Prak,
C.Cabanos,
A.Kimura,
T.Itoh,
B.Mikami,
S.Utsumi,
N.Maruyama.
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Ref.
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Biochim Biophys Acta, 2010,
1804,
1432-1442.
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PubMed id
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Abstract
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The crystal structures of two pro-11S globulins namely: rapeseed procruciferin
and pea prolegumin are presented here. We have extensively compared them with
the other known structures of plant seed 11S and 7S globulins. In general, the
disordered regions in the crystal structures among the 11S globulins correspond
to their five variable regions. Variable region III of procruciferin is
relatively short and is in a loop conformation. This region is highly disordered
in other pro-11S globulin crystals. Local helical and strand variations also
occur across the group despite general structure conservation. We showed how
these variations may alter specific physicochemical, functional and
physiological properties. Aliphatic hydrophobic residues on the molecular
surface correlate well with Tm values of the globulins. We also considered other
structural features that were reported to influence thermal stability but no
definite conclusion was drawn since each factor has additive or subtractive
effect. Comparison between proA3B4 and mature A3B4 revealed an increase in
r.m.s.d. values near variable regions II and IV. Both regions are on the IE
face. Secondary structure based alignment of 11S and 7S globulins revealed 16
identical residues. Based on proA3B4 sequence, Pro60, Gly128, Phe163, Phe208,
Leu213, Leu227, Ile237, Pro382, Val404, Pro425 and Val 466 are involved in
trimer formation and stabilization. Gly28, Gly74, Asp135, Gly349 and Gly397 are
involved in correct globular folding.
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