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PDBsum entry 4mbr
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Protein binding
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PDB id
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4mbr
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PDB id:
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| Name: |
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Protein binding
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Title:
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3.65 angstrom crystal structure of serine-rich repeat protein (srr2) from streptococcus agalactiae
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Structure:
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Serine-rich repeat protein 2. Chain: a. Fragment: unp residues 213-548. Engineered: yes
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Source:
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Streptococcus agalactiae. Organism_taxid: 1311. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.65Å
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R-factor:
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0.215
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R-free:
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0.241
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Authors:
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G.Minasov,L.Shuvalova,I.Dubrovska,J.Winsor,H.S.Seo,R.Seepersaud, K.S.Doran,T.M.Iverson,P.M.Sullam,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
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Key ref:
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H.S.Seo
et al.
(2013).
Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae.
J Biol Chem,
288,
35982-35996.
PubMed id:
DOI:
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Date:
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19-Aug-13
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Release date:
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06-Nov-13
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PROCHECK
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Headers
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References
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Q49RA6
(Q49RA6_STRAG) -
Serine-rich repeat protein 2 from Streptococcus agalactiae
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Seq:
Struc:
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1205 a.a.
316 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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J Biol Chem
288:35982-35996
(2013)
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PubMed id:
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Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae.
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H.S.Seo,
G.Minasov,
R.Seepersaud,
K.S.Doran,
I.Dubrovska,
L.Shuvalova,
W.F.Anderson,
T.M.Iverson,
P.M.Sullam.
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ABSTRACT
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The serine-rich repeat glycoproteins of Gram-positive bacteria comprise a large
family of cell wall proteins. Streptococcus agalactiae (group B streptococcus,
GBS) expresses either Srr1 or Srr2 on its surface, depending on the strain. Srr1
has recently been shown to bind fibrinogen, and this interaction contributes to
the pathogenesis of GBS meningitis. Although strains expressing Srr2 appear to
be hypervirulent, no ligand for this adhesin has been described. We now
demonstrate that Srr2 also binds human fibrinogen and that this interaction
promotes GBS attachment to endothelial cells. Recombinant Srr1 and Srr2 bound
fibrinogen in vitro, with affinities of KD = 2.1 × 10(-5) and 3.7 × 10(-6) m,
respectively, as measured by surface plasmon resonance spectroscopy. The binding
site for Srr1 and Srr2 was localized to tandem repeats 6-8 of the fibrinogen Aα
chain. The structures of both the Srr1 and Srr2 binding regions were determined
and, in combination with mutagenesis studies, suggest that both Srr1 and Srr2
interact with a segment of these repeats via a "dock, lock, and latch"
mechanism. Moreover, properties of the latch region may account for the
increased affinity between Srr2 and fibrinogen. Together, these studies identify
how greater affinity of Srr2 for fibrinogen may contribute to the increased
virulence associated with Srr2-expressing strains.
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Links
