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PDBsum entry 2fu2
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Structural genomics, unknown function
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PDB id
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2fu2
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Contents |
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* Residue conservation analysis
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PDB id:
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Structural genomics, unknown function
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Title:
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Crystal structure of protein spy2152 from streptococcus pyogenes
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Structure:
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Hypothetical protein spy2152. Chain: a. Engineered: yes
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Source:
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Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.15Å
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R-factor:
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0.161
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R-free:
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0.254
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Authors:
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C.Chang,M.Cymborowski,Z.Otwinowski,W.Minor,L.-E.Lezondra,S.Clancy, A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
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Key ref:
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C.Chang
et al.
(2009).
The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes.
Bmc Struct Biol,
9,
75-75.
PubMed id:
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Date:
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25-Jan-06
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Release date:
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07-Mar-06
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PROCHECK
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Headers
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References
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Q48QT2
(Q48QT2_STRPM) -
Bacteriocin from Streptococcus pyogenes serotype M28 (strain MGAS6180)
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Seq: Struc:
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108 a.a.
78 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Bmc Struct Biol
9:75-75
(2009)
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PubMed id:
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The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes.
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C.Chang,
P.Coggill,
A.Bateman,
R.D.Finn,
M.Cymborowski,
Z.Otwinowski,
W.Minor,
L.Volkart,
A.Joachimiak.
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ABSTRACT
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BACKGROUND: Many Gram-positive lactic acid bacteria (LAB) produce anti-bacterial
peptides and small proteins called bacteriocins, which enable them to compete
against other bacteria in the environment. These peptides fall structurally into
three different classes, I, II, III, with class IIa being pediocin-like single
entities and class IIb being two-peptide bacteriocins. Self-protective cognate
immunity proteins are usually co-transcribed with these toxins. Several examples
of cognates for IIa have already been solved structurally. Streptococcus
pyogenes, closely related to LAB, is one of the most common human pathogens, so
knowledge of how it competes against other LAB species is likely to prove
invaluable. RESULTS: We have solved the crystal structure of the gene-product of
locus Spy_2152 from S. pyogenes, (PDB:2fu2), and found it to comprise an
anti-parallel four-helix bundle that is structurally similar to other
bacteriocin immunity proteins. Sequence analyses indicate this protein to be a
possible immunity protein protective against class IIa or IIb bacteriocins.
However, given that S. pyogenes appears to lack any IIa pediocin-like proteins
but does possess class IIb bacteriocins, we suggest this protein confers
immunity to IIb-like peptides. CONCLUSIONS: Combined structural, genomic and
proteomic analyses have allowed the identification and in silico
characterization of a new putative immunity protein from S. pyogenes, possibly
the first structure of an immunity protein protective against potential class
IIb two-peptide bacteriocins. We have named the two pairs of putative
bacteriocins found in S. pyogenes pyogenecin 1, 2, 3 and 4.
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');
}
}
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