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PDBsum entry 1a90
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Thiol protease inhibitor
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PDB id
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1a90
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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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Thiol protease inhibitor
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Title:
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Recombinant mutant chicken egg white cystatin, nmr, 31 structures
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Structure:
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Cystatin. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Organ: egg. Cell: egg. Cellular_location: cytoplasm (white). Expressed in: escherichia coli. Expression_system_taxid: 562
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NMR struc:
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31 models
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Authors:
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T.Dieckmann,L.Mitschang,M.Hofmann,J.Kos,V.Turk,E.A.Auerswald, R.Jaenicke,H.Oschkinat
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Key ref:
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T.Dieckmann
et al.
(1993).
The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.
J Mol Biol,
234,
1048-1059.
PubMed id:
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Date:
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14-Apr-98
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Release date:
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17-Jun-98
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PROCHECK
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Headers
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References
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P01038
(CYT_CHICK) -
Cystatin from Gallus gallus
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Seq:
Struc:
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139 a.a.
108 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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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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J Mol Biol
234:1048-1059
(1993)
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PubMed id:
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The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.
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T.Dieckmann,
L.Mitschang,
M.Hofmann,
J.Kos,
V.Turk,
E.A.Auerswald,
R.Jaenicke,
H.Oschkinat.
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ABSTRACT
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The solution structures of the phosphorylated form of native chicken cystatin
and the recombinant variant AEF-S1M-M29I-M89L were determined by 2D, 3D and
4D-NMR. The structures turn out to be very similar, despite the substitutions
and the phosphorylation of the wild-type. Their dominant feature is a
five-stranded beta-sheet, which is wrapped around a five-turn alpha-helix, as
shown by X-ray crystallographic studies of wild-type chicken cystatin. However,
the NMR analysis shows that the second helix observed in the crystal is not
present in solution. The phosphorylation occurs at S80, which is located in a
flexible region. For this reason, very few effects on the structure are
observed. Comparison of structures of the unphosphorylated variant and the
wild-type shows small effects on H84 which is located in the supposed
recognition site of the serine kinase. This recognition site appears to be well
structured as a large loop-containing bulge of the beta-sheet. The N termini of
both mutants, which contribute to a large extent to the binding to the
proteinase, are very flexible. A loop structure involving the residues L7 to A10
as found in related inhibitors, such as in the kininogen domains 2 and 3, is not
sufficiently populated to be observed.
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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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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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S.Zhu,
L.Wei,
K.Yamasaki,
and
R.L.Gallo
(2008).
Activation of cathepsin L by the cathelin-like domain of protegrin-3.
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Mol Immunol,
45,
2531-2536.
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S.Zhu
(2008).
Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor?
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Trends Microbiol,
16,
353-360.
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A.W.Schüttelkopf,
G.Hamilton,
C.Watts,
and
D.M.van Aalten
(2006).
Structural basis of reduction-dependent activation of human cystatin F.
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J Biol Chem,
281,
16570-16575.
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PDB code:
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J.He,
Y.Song,
N.Ueyama,
A.Saito,
H.Azakami,
and
A.Kato
(2006).
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast.
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Protein Sci,
15,
213-222.
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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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S.Cui,
S.Nikolovski,
K.Nanayakkara,
and
L.Selwood
(2005).
VAP1, with cystatin C motif, an oocyte protein encoded by a novel ovarian-specific gene during oogenesis in the common brushtail possum (Trichosurus vulpecula).
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Mol Reprod Dev,
71,
19-28.
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Y.C.Su,
J.C.Lin,
and
H.L.Liu
(2005).
Homology model and molecular dynamics simulation of carp ovum cystatin.
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Biotechnol Prog,
21,
1315-1320.
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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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A.Pavlova,
and
I.Björk
(2002).
The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.
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Eur J Biochem,
269,
5649-5658.
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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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M.Calero,
M.Pawlik,
C.Soto,
E.M.Castaño,
E.M.Sigurdsson,
A.Kumar,
G.Gallo,
B.Frangione,
and
E.Levy
(2001).
Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
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J Neurochem,
77,
628-637.
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K.Nagata,
N.Kudo,
K.Abe,
S.Arai,
and
M.Tanokura
(2000).
Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
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Biochemistry,
39,
14753-14760.
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PDB code:
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R.A.Staniforth,
J.L.Dean,
Q.Zhong,
E.Zerovnik,
A.R.Clarke,
and
J.P.Waltho
(2000).
The major transition state in folding need not involve the immobilization of side chains.
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Proc Natl Acad Sci U S A,
97,
5790-5795.
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S.Akashi,
and
K.Takio
(2000).
Characterization of the interface structure of enzyme-inhibitor complex by using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
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Protein Sci,
9,
2497-2505.
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S.Estrada,
S.T.Olson,
E.Raub-Segall,
and
I.Björk
(2000).
The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter group.
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Protein Sci,
9,
2218-2224.
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M.Alvarez-Fernandez,
A.J.Barrett,
B.Gerhartz,
P.M.Dando,
J.Ni,
and
M.Abrahamson
(1999).
Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site.
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J Biol Chem,
274,
19195-19203.
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M.Kozak,
E.Jankowska,
R.Janowski,
Z.Grzonka,
A.Grubb,
M.Alvarez Fernandez,
M.Abrahamson,
and
M.Jaskolski
(1999).
Expression of a selenomethionyl derivative and preliminary crystallographic studies of human cystatin C.
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Acta Crystallogr D Biol Crystallogr,
55,
1939-1942.
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S.Estrada,
A.Pavlova,
and
I.Björk
(1999).
The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain, cathepsin B, and cathepsin L.
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Biochemistry,
38,
7339-7345.
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B.Gerhartz,
I.Ekiel,
and
M.Abrahamson
(1998).
Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.
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Biochemistry,
37,
17309-17317.
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E.Zerovnik,
R.Jerala,
R.Virden,
L.Kroon Zitko,
V.Turk,
and
J.P.Waltho
(1998).
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states.
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Proteins,
32,
304-313.
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S.Estrada,
M.Nycander,
N.J.Hill,
C.J.Craven,
J.P.Waltho,
and
I.Björk
(1998).
The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.
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Biochemistry,
37,
7551-7560.
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S.Halfon,
J.Ford,
J.Foster,
L.Dowling,
L.Lucian,
M.Sterling,
Y.Xu,
M.Weiss,
M.Ikeda,
D.Liggett,
A.Helms,
C.Caux,
S.Lebecque,
C.Hannum,
S.Menon,
T.McClanahan,
D.Gorman,
and
G.Zurawski
(1998).
Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells.
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J Biol Chem,
273,
16400-16408.
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G.Sotiropoulou,
A.Anisowicz,
and
R.Sager
(1997).
Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer.
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J Biol Chem,
272,
903-910.
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M.Mittag,
and
H.Waltenberger
(1997).
In vitro mutagenesis of binding site elements for the clock-controlled proteins CCTR and Chlamy 1.
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Biol Chem,
378,
1167-1170.
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W.Baumeister,
Z.Cejka,
M.Kania,
and
E.Seemüller
(1997).
The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
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Biol Chem,
378,
121-130.
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E.A.Auerswald,
D.K.Nägler,
S.Gross,
I.Assfalg-Machleidt,
M.T.Stubbs,
C.Eckerskorn,
W.Machleidt,
and
H.Fritz
(1996).
Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.
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Eur J Biochem,
235,
534-542.
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I.Olafsson,
L.Thorsteinsson,
and
O.Jensson
(1996).
The molecular pathology of hereditary cystatin C amyloid angiopathy causing brain hemorrhage.
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Brain Pathol,
6,
121-126.
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A.Hall,
K.Håkansson,
R.W.Mason,
A.Grubb,
and
M.Abrahamson
(1995).
Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases.
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J Biol Chem,
270,
5115-5121.
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B.Hu,
L.Coulson,
B.Moyer,
and
P.A.Price
(1995).
Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors.
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J Biol Chem,
270,
431-436.
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G.Lalmanach,
C.Serveau,
M.Brillard-Bourdet,
J.R.Chagas,
R.Mayer,
L.Juliano,
and
F.Gauthier
(1995).
Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases.
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J Protein Chem,
14,
645-653.
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K.Pullen,
P.Rajagopal,
B.R.Branchini,
M.E.Huffine,
J.Reizer,
M.H.Saier,
J.M.Scholtz,
and
R.E.Klevit
(1995).
Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure.
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Protein Sci,
4,
2478-2486.
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E.A.Auerswald,
D.K.Nägler,
A.J.Schulze,
R.A.Engh,
G.Genenger,
W.Machleidt,
and
H.Fritz
(1994).
Production, inhibitory activity, folding and conformational analysis of an N-terminal and an internal deletion variant of chicken cystatin.
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Eur J Biochem,
224,
407-415.
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J.R.Martin,
R.Jerala,
L.Kroon-Zitko,
E.Zerovnik,
V.Turk,
and
J.P.Waltho
(1994).
Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.
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Eur J Biochem,
225,
1181-1194.
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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
code is
shown on the right.
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Links
