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PDBsum entry 1l0q
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Protein binding
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PDB id
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1l0q
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein binding
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Title:
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Tandem yvtn beta-propeller and pkd domains from an archaeal surface layer protein
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Structure:
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Surface layer protein. Chain: a, b, c, d. Fragment: yvtn beta-propeller domain 1 and pkd domain 1. Engineered: yes
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Source:
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Methanosarcina mazei. Organism_taxid: 213585. Strain: s-6. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.40Å
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R-factor:
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0.214
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R-free:
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0.263
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Authors:
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H.Jing,J.Takagi,J.-H.Liu,S.Lindgren,R.-G.Zhang,A.Joachimiak,J.- H.Wang,T.A.Springer
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Key ref:
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H.Jing
et al.
(2002).
Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins.
Structure,
10,
1453-1464.
PubMed id:
DOI:
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Date:
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12-Feb-02
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Release date:
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06-Nov-02
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PROCHECK
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Headers
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References
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Q50245
(Q50245_METMZ) -
ORF492 from Methanosarcina mazei
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Seq: Struc:
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491 a.a.
391 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 1 residue position (black
cross)
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DOI no:
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Structure
10:1453-1464
(2002)
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PubMed id:
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Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins.
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H.Jing,
J.Takagi,
J.H.Liu,
S.Lindgren,
R.G.Zhang,
A.Joachimiak,
J.H.Wang,
T.A.Springer.
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ABSTRACT
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The surface layer of archaeobacteria protects cells from extreme environments
and, in Methanosarcina, may regulate cell adhesion. We identify three domain
types that account for the complete architecture of numerous Methanosarcina
surface layer proteins (SLPs). We solve the crystal structure for two of these
domains, which correspond to the two N-terminal domains of an M. mazei SLP. One
domain displays a unique, highly symmetrical, seven-bladed beta propeller fold,
and the other belongs to the polycystic kidney disease (PKD) superfamily fold.
The third domain is predicted to adopt a beta helix fold. These domains have
homologs in metazoan cell surface proteins, suggesting remarkable relationships
between domains in archaeal SLPs and metazoan cell surface proteins.
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Selected figure(s)
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Figure 1.
Figure 1. Overall Structure(A) Schematic domain structure
of the full-length M. mazei SLP.(B) Ribbons diagram of YVTN b
propeller (magenta) and PKD (blue) domains as viewed from the
top of the b propeller domain. Domain linkers, white; bulge on
strand 1 of W7, green.(C) Side view of the Ca traces of four
molecules in the asymmetric unit, superimposed on the b
propeller domain.(D) Charges on the bumpy bottom surface of the
b propeller domain. The GRASP representation of surface charge
is colored from red ( -10 kEV) to blue (+10 kEV). The view is
vert,
similar 90 degrees from (C) and vert,
similar 180 degrees from (B).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1453-1464)
copyright 2002.
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Figure was
selected
by an automated process.
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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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F.Santos,
P.Yarza,
V.Parro,
C.Briones,
and
J.Antón
(2010).
The metavirome of a hypersaline environment.
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Environ Microbiol,
12,
2965-2976.
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J.J.Margolis,
S.El-Etr,
L.M.Joubert,
E.Moore,
R.Robison,
A.Rasley,
A.M.Spormann,
and
D.M.Monack
(2010).
Contributions of Francisella tularensis subsp. novicida chitinases and Sec secretion system to biofilm formation on chitin.
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Appl Environ Microbiol,
76,
596-608.
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L.M.Teixeira,
A.Strickland,
S.S.Mark,
M.Bergkvist,
Y.Sierra-Sastre,
and
C.A.Batt
(2010).
Entropically driven self-assembly of Lysinibacillus sphaericus S-layer proteins analyzed under various environmental conditions.
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Macromol Biosci,
10,
147-155.
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T.Sathaliyawala,
M.Z.Islam,
Q.Li,
A.Fokine,
M.G.Rossmann,
and
V.B.Rao
(2010).
Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages.
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Mol Microbiol,
77,
444-455.
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A.Veith,
A.Klingl,
B.Zolghadr,
K.Lauber,
R.Mentele,
F.Lottspeich,
R.Rachel,
S.V.Albers,
and
A.Kletzin
(2009).
Acidianus, Sulfolobus and Metallosphaera surface layers: structure, composition and gene expression.
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Mol Microbiol,
73,
58-72.
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D.R.Francoleon,
P.Boontheung,
Y.Yang,
U.Kin,
A.J.Ytterberg,
P.A.Denny,
P.C.Denny,
J.A.Loo,
R.P.Gunsalus,
and
R.R.Loo
(2009).
S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei.
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J Proteome Res,
8,
1972-1982.
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J.R.Forman,
Z.T.Yew,
S.Qamar,
R.N.Sandford,
E.Paci,
and
J.Clarke
(2009).
Non-native interactions are critical for mechanical strength in PKD domains.
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Structure,
17,
1582-1590.
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L.Ma,
M.Xu,
J.R.Forman,
J.Clarke,
and
A.F.Oberhauser
(2009).
Naturally occurring mutations alter the stability of polycystin-1 polycystic kidney disease (PKD) domains.
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J Biol Chem,
284,
32942-32949.
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M.C.Hogan,
L.Manganelli,
J.R.Woollard,
A.I.Masyuk,
T.V.Masyuk,
R.Tammachote,
B.Q.Huang,
A.A.Leontovich,
T.G.Beito,
B.J.Madden,
M.C.Charlesworth,
V.E.Torres,
N.F.LaRusso,
P.C.Harris,
and
C.J.Ward
(2009).
Characterization of PKD protein-positive exosome-like vesicles.
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J Am Soc Nephrol,
20,
278-288.
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R.P.Fagan,
D.Albesa-Jové,
O.Qazi,
D.I.Svergun,
K.A.Brown,
and
N.F.Fairweather
(2009).
Structural insights into the molecular organization of the S-layer from Clostridium difficile.
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Mol Microbiol,
71,
1308-1322.
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PDB code:
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A.Baba-Dikwa,
D.Thompson,
N.J.Spencer,
S.C.Andrews,
and
K.A.Watson
(2008).
Overproduction, purification and preliminary X-ray diffraction analysis of YncE, an iron-regulated Sec-dependent periplasmic protein from Escherichia coli.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
966-969.
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F.J.Stevens
(2008).
Homology versus analogy: possible evolutionary relationship of immunoglobulins, cupredoxins, and Cu,Zn-superoxide dismutase.
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J Mol Recognit,
21,
20-29.
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I.Chaudhuri,
J.Söding,
and
A.N.Lupas
(2008).
Evolution of the beta-propeller fold.
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Proteins,
71,
795-803.
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T.Pavkov,
E.M.Egelseer,
M.Tesarz,
D.I.Svergun,
U.B.Sleytr,
and
W.Keller
(2008).
The structure and binding behavior of the bacterial cell surface layer protein SbsC.
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Structure,
16,
1226-1237.
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PDB code:
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C.D.Krause,
Z.H.Yang,
Y.S.Kim,
J.H.Lee,
J.R.Cook,
and
S.Pestka
(2007).
Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential.
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Pharmacol Ther,
113,
50-87.
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F.Reiter,
M.Hartl,
A.I.Karagiannidis,
and
K.Bister
(2007).
WS5, a direct target of oncogenic transcription factor Myc, is related to human melanoma glycoprotein genes and has oncogenic potential.
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Oncogene,
26,
1769-1779.
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J.Kubrycht,
K.Sigler,
M.Růzicka,
P.Soucek,
J.Borecký,
and
P.Jezek
(2006).
Ancient phylogenetic beginnings of immunoglobulin hypermutation.
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J Mol Evol,
63,
691-706.
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S.E.Haydel,
and
J.E.Clark-Curtiss
(2006).
The Mycobacterium tuberculosis TrcR response regulator represses transcription of the intracellularly expressed Rv1057 gene, encoding a seven-bladed beta-propeller.
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J Bacteriol,
188,
150-159.
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H.Claus,
E.Akça,
T.Debaerdemaeker,
C.Evrard,
J.P.Declercq,
J.R.Harris,
B.Schlott,
and
H.König
(2005).
Molecular organization of selected prokaryotic S-layer proteins.
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Can J Microbiol,
51,
731-743.
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F.J.Stevens
(2004).
Amyloid formation: an emulation of matrix protein assembly?
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Amyloid,
11,
232-244.
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S.Adindla,
K.K.Inampudi,
K.Guruprasad,
and
L.Guruprasad
(2004).
Identification and analysis of novel tandem repeats in the cell surface proteins of archaeal and bacterial genomes using computational tools.
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Comp Funct Genomics,
5,
2.
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S.Cheek,
Y.Qi,
S.S.Krishna,
L.N.Kinch,
and
N.V.Grishin
(2004).
4SCOPmap: automated assignment of protein structures to evolutionary superfamilies.
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BMC Bioinformatics,
5,
197.
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T.Pavkov,
M.Oberer,
E.M.Egelseer,
M.Sára,
U.B.Sleytr,
and
W.Keller
(2003).
Crystallization and preliminary structure determination of the C-terminal truncated domain of the S-layer protein SbsC.
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Acta Crystallogr D Biol Crystallogr,
59,
1466-1468.
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R.W.Pickersgill
(2002).
Complex cell signaling molecules from ancient molecular glue.
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Structure,
10,
1287-1288.
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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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}
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