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Immune system
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PDB id
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3c2x
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Crystal structure of peptidoglycan recognition protein at 1. Resolution
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Structure:
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Peptidoglycan recognition protein. Chain: a, b, c, d. Synonym: peptidoglycan recognition protein short, pgrp-s
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Source:
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Camelus dromedarius. Arabian camel. Organism_taxid: 9838
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Resolution:
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1.83Å
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R-factor:
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0.225
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R-free:
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0.247
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Authors:
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P.Sharma,N.Singh,M.Sinha,S.Sharma,M.Perbandt,C.Betzel,P.Kaur A.Srinivasan,T.P.Singh
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Key ref:
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P.Sharma
et al.
(2008).
Crystal structure of the peptidoglycan recognition protein at 1.8 A resolution reveals dual strategy to combat infection through two independent functional homodimers.
J Mol Biol,
378,
921-930.
PubMed id:
DOI:
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Date:
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26-Jan-08
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Release date:
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25-Mar-08
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PROCHECK
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Headers
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References
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Q9GK12
(PGRP1_CAMDR) -
Peptidoglycan recognition protein 1
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Seq:
Struc:
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193 a.a.
171 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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1 term
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Biological process
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innate immune response
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3 terms
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Biochemical function
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peptidoglycan binding
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3 terms
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DOI no:
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J Mol Biol
378:921-930
(2008)
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PubMed id:
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Crystal structure of the peptidoglycan recognition protein at 1.8 A resolution reveals dual strategy to combat infection through two independent functional homodimers.
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P.Sharma,
N.Singh,
M.Sinha,
S.Sharma,
M.Perbandt,
C.Betzel,
P.Kaur,
A.Srinivasan,
T.P.Singh.
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ABSTRACT
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The mammalian peptidoglycan recognition protein-S (PGRP-S) binds to
peptidoglycans (PGNs), which are essential components of the cell wall of
bacteria. The protein was isolated from the samples of milk obtained from camels
with mastitis and purified to homogeneity and crystallized. The crystals belong
to orthorhombic space group I222 with a=87.0 A, b=101.7 A and c=162.3 A having
four crystallographically independent molecules in the asymmetric unit. The
structure has been determined using X-ray crystallographic data and refined to
1.8 A resolution. Overall, the structures of all the four crystallographically
independent molecules are identical. The folding of PGRP-S consists of a central
beta-sheet with five beta-strands, four parallel and one antiparallel, and three
alpha-helices. This protein fold provides two functional sites. The first of
these is the PGN-binding site, located on the groove that opens on the surface
in the direction opposite to the location of the N terminus. The second site is
implicated to be involved in the binding of non-PGN molecules, it also includes
putative N-terminal segment residues (1-31) and helix alpha2 in the extended
binding. The structure reveals a novel arrangement of PGRP-S molecules in which
two pairs of molecules associate to form two independent dimers. The first dimer
is formed by two molecules with N-terminal segments at the interface in which
non-PGN binding sites are buried completely, whereas the PGN-binding sites of
two participating molecules are fully exposed at the opposite ends of the dimer.
In the second dimer, PGN-binding sites are buried at the interface while non-PGN
binding sites are fully exposed at the opposite ends of the dimer. This form of
dimeric arrangement is unique and seems to be aimed at enhancing the capability
of the protein against specific invading bacteria. This mode of functional
dimerization enhances efficiency and specificity, and is observed for the first
time in the family of PGRP molecules.
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Selected figure(s)
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Figure 1.
Fig. 1. The two dimers are drawn to indicate the PGN and
non-PGN-binding sites. (a) In dimer 1, the two PGN-binding sites
are indicated in green, while non-PGN-binding sites are buried
at the interface in yellow (b) in dimer 2, the reverse is the
case. O indicates the position of the 2-fold axis perpendicular
to the plane of the paper.
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Figure 4.
Fig. 4. The hydrogen bonded interactions at the interface of
two dimers: (a) the A–B dimer; (b) the C–D dimer.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2008,
378,
921-930)
copyright 2008.
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Figures were
selected
by an automated process.
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Links
