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PDBsum entry 1eqk
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Hydrolase inhibitor
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PDB id
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1eqk
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase inhibitor
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Title:
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Solution structure of oryzacystatin-i, a cysteine proteinase inhibitor of the rice, oryza sativa l. Japonica
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Structure:
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Oryzacystatin-i. Chain: a. Engineered: yes
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Source:
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Oryza sativa japonica group. Organism_taxid: 39947. Strain: japonica group. Tissue: seed. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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21 models
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Authors:
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K.Nagata,N.Kudo,K.Abe,S.Arai,M.Tanokura
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Key ref:
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K.Nagata
et al.
(2000).
Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
Biochemistry,
39,
14753-14760.
PubMed id:
DOI:
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Date:
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05-Apr-00
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Release date:
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10-Jan-01
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PROCHECK
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Headers
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References
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P09229
(CYT1_ORYSJ) -
Cysteine proteinase inhibitor 1 from Oryza sativa subsp. japonica
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Seq:
Struc:
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140 a.a.
102 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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Biochemistry
39:14753-14760
(2000)
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PubMed id:
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Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
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K.Nagata,
N.Kudo,
K.Abe,
S.Arai,
M.Tanokura.
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ABSTRACT
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The three-dimensional structure of oryzacystatin-I, a cysteine proteinase
inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution
at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body
(Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an alpha-helix
and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions
(Ser2-Val12 and Ala98-Ala102) are less defined. The helix-sheet architechture of
oryzacystatin-I is stabilized by a hydrophobic cluster formed between the
alpha-helix and the beta-sheet and is considerably similar to that of monellin,
a sweet-tasting protein from an African berry, as well as those of the animal
cystatins studied, e.g., chicken egg white cystatin and human stefins A and B
(also referred to as human cystatins A and B). Detailed structural comparison
indicates that oryzacystatin-I is more similar to chicken cystatin, which
belongs to the type-2 animal cystatins, than to human stefins A and B, which
belong to the type-1 animal cystatins, despite different loop length.
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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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K.Nagata
(2010).
Studies of the structure-activity relationships of peptides and proteins involved in growth and development based on their three-dimensional structures.
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Biosci Biotechnol Biochem,
74,
462-470.
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N.F.Valadares,
M.Dellamano,
A.Soares-Costa,
F.Henrique-Silva,
and
R.C.Garratt
(2010).
Molecular determinants of improved cathepsin B inhibition by new cystatins obtained by DNA shuffling.
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BMC Struct Biol,
10,
30.
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D.Kordis,
and
V.Turk
(2009).
Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes.
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BMC Evol Biol,
9,
266.
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K.Doi-Kawano,
E.Nishimoto,
Y.Kouzuma,
D.Takahashi,
S.Yamashita,
and
M.Kimura
(2009).
Steady-state and time-resolved fluorescence spectroscopic studies on interaction of the N-terminal region with the hairpin loop of the phytocystatin Scb.
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J Fluoresc,
19,
631-639.
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S.Rodziewicz-Motowidło,
J.Iwaszkiewicz,
R.Sosnowska,
P.Czaplewska,
E.Sobolewski,
A.Szymańska,
K.Stachowiak,
and
A.Liwo
(2009).
The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants.
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Biopolymers,
91,
373-383.
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K.Abe
(2008).
Studies on taste: molecular biology and food science.
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Biosci Biotechnol Biochem,
72,
1647-1656.
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K.M.Wang,
S.Kumar,
Y.S.Cheng,
S.Venkatagiri,
A.H.Yang,
and
K.W.Yeh
(2008).
Characterization of inhibitory mechanism and antifungal activity between group-1 and group-2 phytocystatins from taro (Colocasia esculenta).
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FEBS J,
275,
4980-4989.
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C.Girard,
D.Rivard,
A.Kiggundu,
K.Kunert,
S.C.Gleddie,
C.Cloutier,
and
D.Michaud
(2007).
A multicomponent, elicitor-inducible cystatin complex in tomato, Solanum lycopersicum.
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New Phytol,
173,
841-851.
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A.Kiggundu,
M.C.Goulet,
C.Goulet,
J.F.Dubuc,
D.Rivard,
M.Benchabane,
G.Pépin,
C.van der Vyver,
K.Kunert,
and
D.Michaud
(2006).
Modulating the proteinase inhibitory profile of a plant cystatin by single mutations at positively selected amino acid sites.
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Plant J,
48,
403-413.
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J.T.Christeller,
P.C.Farley,
R.K.Marshall,
A.Anandan,
M.M.Wright,
R.D.Newcomb,
and
W.A.Laing
(2006).
The squash aspartic proteinase inhibitor SQAPI is widely present in the cucurbitales, comprises a small multigene family, and is a member of the phytocystatin family.
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J Mol Evol,
63,
747-757.
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F.Brunelle,
C.Girard,
C.Cloutier,
and
D.Michaud
(2005).
A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine digestive proteinases.
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Arch Insect Biochem Physiol,
60,
20-31.
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M.Alvarez-Fernandez,
Y.H.Liang,
M.Abrahamson,
and
X.D.Su
(2005).
Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.
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J Biol Chem,
280,
18221-18228.
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PDB codes:
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M.Martínez,
Z.Abraham,
P.Carbonero,
and
I.Díaz
(2005).
Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley.
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Mol Genet Genomics,
273,
423-432.
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D.J.Shyu,
C.L.Chyan,
J.T.Tzen,
and
W.M.Chou
(2004).
Molecular cloning, expression, and functional characterization of a cystatin from pineapple stem.
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Biosci Biotechnol Biochem,
68,
1681-1689.
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B.Belenghi,
F.Acconcia,
M.Trovato,
M.Perazzolli,
A.Bocedi,
F.Polticelli,
P.Ascenzi,
and
M.Delledonne
(2003).
AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell death.
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Eur J Biochem,
270,
2593-2604.
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M.Martínez,
E.López-Solanilla,
P.Rodríguez-Palenzuela,
P.Carbonero,
and
I.Díaz
(2003).
Inhibition of plant-pathogenic fungi by the barley cystatin Hv-CPI (gene Icy) is not associated with its cysteine-proteinase inhibitory properties.
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Mol Plant Microbe Interact,
16,
876-883.
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J.F.Sanchez,
F.Wojcik,
Y.S.Yang,
M.P.Strub,
J.M.Strub,
A.Van Dorsselaer,
M.Martin,
R.Lehrer,
T.Ganz,
A.Chavanieu,
B.Calas,
and
A.Aumelas
(2002).
Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor.
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Biochemistry,
41,
21-30.
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S.Arai
(2002).
Global view on functional foods: Asian perspectives.
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Br J Nutr,
88,
S139-S143.
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Y.Sawano,
T.Muramatsu,
K.Hatano,
K.Nagata,
and
M.Tanokura
(2002).
Characterization of genomic sequence coding for bromelain inhibitors in pineapple and expression of its recombinant isoform.
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J Biol Chem,
277,
28222-28227.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
