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PDBsum entry 2w9q
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Hydrolase inhibitor
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PDB id
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2w9q
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Hydrolase inhibitor
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Title:
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Crystal structure of potato multicystatin-p212121
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Structure:
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Multicystatin. Chain: a. Fragment: residues 100-186. Synonym: potato multicystatin, mc. Engineered: yes
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Source:
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Solanum tuberosum. Potato. Organism_taxid: 4113. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.50Å
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R-factor:
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0.193
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R-free:
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0.232
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Authors:
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M.S.Nissen,G.N.Kumar,B.Youn,D.B.Knowles,K.S.Lam,W.J.Ballinger, N.R.Knowles,C.Kang
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Key ref:
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M.S.Nissen
et al.
(2009).
Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins.
Plant Cell,
21,
861-875.
PubMed id:
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Date:
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28-Jan-09
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Release date:
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02-Feb-10
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PROCHECK
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Headers
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References
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P37842
(CYTM_SOLTU) -
Multicystatin from Solanum tuberosum
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Seq:
Struc:
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756 a.a.
87 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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Plant Cell
21:861-875
(2009)
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PubMed id:
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Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins.
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M.S.Nissen,
G.N.Kumar,
B.Youn,
D.B.Knowles,
K.S.Lam,
W.J.Ballinger,
N.R.Knowles,
C.Kang.
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ABSTRACT
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Potato (Solanum tuberosum) multicystatin (PMC) is a crystalline Cys protease
inhibitor present in the subphellogen layer of potato tubers. It consists of
eight tandem domains of similar size and sequence. Our in vitro results showed
that the pH/PO(4)(-)-dependent oligomeric behavior of PMC was due to its
multidomain nature and was not a characteristic of the individual domains. Using
a single domain of PMC, which still maintains inhibitor activity, we identified
a target protein of PMC, a putative Cys protease. In addition, our crystal
structure of a representative repeating unit of PMC, PMC-2, showed structural
similarity to both type I and type II cystatins. The N-terminal trunk,
alpha-helix, and L2 region of PMC-2 were most similar to those of type I
cystatins, while the conformation of L1 more closely resembled that of type II
cystatins. The structure of PMC-2 was most similar to the intensely sweet
protein monellin from Dioscorephyllum cumminisii (serendipity berry), despite a
low level of sequence similarity. We present a model for the possible molecular
organization of the eight inhibitory domains in crystalline PMC. The unique
molecular properties of the oligomeric PMC crystal are discussed in relation to
its potential function in regulating the activity of proteases in potato tubers.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Carrillo,
M.Martinez,
F.Alvarez-Alfageme,
P.Castañera,
G.Smagghe,
I.Diaz,
and
F.Ortego
(2011).
A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants.
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Transgenic Res,
20,
305-319.
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L.Carrillo,
M.Martinez,
K.Ramessar,
I.Cambra,
P.Castañera,
F.Ortego,
and
I.Díaz
(2011).
Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases.
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Plant Cell Rep,
30,
101-112.
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O.Szczepankiewicz,
C.Cabaleiro-Lago,
G.G.Tartaglia,
M.Vendruscolo,
T.Hunter,
G.J.Hunter,
H.Nilsson,
E.Thulin,
and
S.Linse
(2011).
Interactions in the native state of monellin, which play a protective role against aggregation.
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Mol Biosyst,
7,
521-532.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
