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PDBsum entry 2ww8
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Cell adhesion
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PDB id
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2ww8
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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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Cell adhesion
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Title:
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Structure of the pilus adhesin (rrga) from streptococcus pneumoniae
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Structure:
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Cell wall surface anchor family protein. Chain: a. Synonym: rrga. Engineered: yes. Other_details: isopeptide-bond links k191 and n695, k742 and n854
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Source:
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Streptococcus pneumoniae. Organism_taxid: 1313. Strain: tigr 4. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: ril.
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Resolution:
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1.90Å
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R-factor:
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0.197
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R-free:
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0.235
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Authors:
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T.Izore,C.Contreras-Martel,L.El-Mortaji,C.Manzano,R.Terrasse, T.Vernet,A.M.Di-Guilmi,A.Dessen
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Key ref:
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T.Izoré
et al.
(2010).
Structural basis of host cell recognition by the pilus adhesin from Streptococcus pneumoniae.
Structure,
18,
106-115.
PubMed id:
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Date:
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22-Oct-09
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Release date:
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19-Jan-10
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PROCHECK
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Headers
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References
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A0A0H2UNT6
(A0A0H2UNT6_STRPN) -
Cell wall surface anchor family protein from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
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Seq:
Struc:
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893 a.a.
815 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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Structure
18:106-115
(2010)
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PubMed id:
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Structural basis of host cell recognition by the pilus adhesin from Streptococcus pneumoniae.
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T.Izoré,
C.Contreras-Martel,
L.El Mortaji,
C.Manzano,
R.Terrasse,
T.Vernet,
A.M.Di Guilmi,
A.Dessen.
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ABSTRACT
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Pili are fibrous virulence factors associated directly to the bacterial surface
that play critical roles in adhesion and recognition of host cell receptors. The
human pathogen Streptococcus pneumoniae carries a single pilus-related adhesin
(RrgA) that is key for infection establishment and provides protection from
bacterial challenge in animal infection models, but details of these roles
remain unclear. Here we report the high-resolution crystal structure of RrgA, a
893-residue elongated macromolecule whose fold contains four domains presenting
both eukaryotic and prokaryotic origins. RrgA harbors an integrin I
collagen-recognition domain decorated with two inserted "arms" that fold into a
positively charged cradle, as well as three "stalk-forming" domains. We show by
site-specific mutagenesis, mass spectrometry, and thermal shift assays that
intradomain isopeptide bonds play key roles in stabilizing RrgA's stalk. The
high sequence similarity between RrgA and its homologs in other Gram-positive
microorganisms suggests common strategies for ECM recognition and immune evasion.
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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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A.P.Hendrickx,
J.M.Budzik,
S.Y.Oh,
and
O.Schneewind
(2011).
Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds.
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Nat Rev Microbiol,
9,
166-176.
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H.J.Kang,
and
E.N.Baker
(2011).
Intramolecular isopeptide bonds: protein crosslinks built for stress?
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Trends Biochem Sci,
36,
229-237.
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J.Löfling,
V.Vimberg,
P.Battig,
and
B.Henriques-Normark
(2011).
Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues.
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Cell Microbiol,
13,
186-197.
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K.Vengadesan,
and
S.V.Narayana
(2011).
Structural biology of Gram-positive bacterial adhesins.
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Protein Sci,
20,
759-772.
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K.Vengadesan,
X.Ma,
P.Dwivedi,
H.Ton-That,
and
S.V.Narayana
(2011).
A model for group B Streptococcus pilus type 1: the structure of a 35-kDa C-terminal fragment of the major pilin GBS80.
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J Mol Biol,
407,
731-743.
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PDB codes:
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M.Moschioni,
C.Emolo,
M.Biagini,
S.Maccari,
W.Pansegrau,
C.Donati,
M.Hilleringmann,
I.Ferlenghi,
P.Ruggiero,
A.Sinisi,
M.Pizza,
N.Norais,
M.A.Barocchi,
and
V.Masignani
(2010).
The two variants of the Streptococcus pneumoniae pilus 1 RrgA adhesin retain the same function and elicit cross-protection in vivo.
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Infect Immun,
78,
5033-5042.
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R.Liddington
(2010).
Catching pneumonia.
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Structure,
18,
6-8.
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W.D.Smith,
J.A.Pointon,
E.Abbot,
H.J.Kang,
E.N.Baker,
B.H.Hirst,
J.A.Wilson,
M.J.Banfield,
and
M.A.Kehoe
(2010).
Roles of minor pilin subunits Spy0125 and Spy0130 in the serotype M1 Streptococcus pyogenes strain SF370.
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J Bacteriol,
192,
4651-4659.
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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
