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PDBsum entry 4pph
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Plant protein
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PDB id
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4pph
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PDB id:
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| Name: |
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Plant protein
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Title:
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Crystal structure of conglutin gamma, a unique basic 7s globulin from lupine seeds
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Structure:
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Conglutin gamma. Chain: a, b, c, d, e, f. Fragment: lupinus angustifolius conglutin gamma,unp residues 33-449. Synonym: conglutin gamma 1
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Source:
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Lupinus angustifolius. Narrow-leaved blue lupin. Organism_taxid: 3871
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Resolution:
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2.01Å
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R-factor:
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0.146
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R-free:
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0.174
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Authors:
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J.Czubinski,J.Barciszewski,M.Gilski,E.Lampart-Szczapa,M.Jaskolski
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Key ref:
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J.Czubinski
et al.
(2015).
Structure of γ-conglutin: insight into the quaternary structure of 7S basic globulins from legumes.
Acta Crystallogr D Biol Crystallogr,
71,
224-238.
PubMed id:
DOI:
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Date:
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27-Feb-14
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Release date:
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11-Feb-15
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PROCHECK
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Headers
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References
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Q42369
(CONG1_LUPAN) -
Gamma conglutin 1 from Lupinus angustifolius
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Seq:
Struc:
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449 a.a.
390 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:224-238
(2015)
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PubMed id:
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Structure of γ-conglutin: insight into the quaternary structure of 7S basic globulins from legumes.
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J.Czubinski,
J.Barciszewski,
M.Gilski,
K.Szpotkowski,
J.Debski,
E.Lampart-Szczapa,
M.Jaskolski.
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ABSTRACT
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γ-Conglutin from lupin seeds is an unusual 7S basic globulin protein. It is
capable of reducing glycaemia in mammals, but the structural basis of this
activity is not known. γ-Conglutin shares a high level of structural homology
with glycoside hydrolase inhibitor proteins, although it lacks any kind of
inhibitory activity against plant cell-wall degradation enzymes. In addition,
γ-conglutin displays a less pronounced structural similarity to pepsin-like
aspartic proteases, but it is proteolytically dysfunctional. Only one structural
study of a legume 7S basic globulin, that isolated from soybean, has been
reported to date. The quaternary assembly of soybean 7S basic globulin (Bg7S) is
arranged as a cruciform-shaped tetramer comprised of two superposed dimers.
Here, the crystal structure of γ-conglutin isolated from Lupinus angustifolius
seeds (LangC) is presented. The polypeptide chain of LangC is
post-translationally cleaved into α and β subunits but retains its covalent
integrity owing to a disulfide bridge. The protomers of LangC undergo an
intricate quaternary assembly, resulting in a ring-like hexamer with
noncrystallographic D3 symmetry. The twofold-related dimers are similar to those
in Bg7S but their assembly is different as a consequence of mutations in a
β-strand that is involved in intermolecular β-sheet formation in γ-conglutin.
Structural elucidation of γ-conglutin will help to explain its physiological
role, especially in the evolutionary context, and will guide further research
into the hypoglycaemic activity of this protein in humans, with potential
consequences for novel antidiabetic therapies.
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