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PDBsum entry 4oxd
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Contents |
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185 a.a.
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167 a.a.
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171 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of the ldcb ld-Carboxypeptidase reveals the molecular basis of peptidoglycan recognition.
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Authors
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C.N.Hoyland,
C.Aldridge,
R.M.Cleverley,
M.C.Duchêne,
G.Minasov,
O.Onopriyenko,
K.Sidiq,
P.J.Stogios,
W.F.Anderson,
R.A.Daniel,
A.Savchenko,
W.Vollmer,
R.J.Lewis.
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Ref.
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Structure, 2014,
22,
949-960.
[DOI no: ]
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PubMed id
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Abstract
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Peptidoglycan surrounds the bacterial cytoplasmic membrane to protect the cell
against osmolysis. The biosynthesis of peptidoglycan, made of glycan strands
crosslinked by short peptides, is the target of antibiotics like β-lactams and
glycopeptides. Nascent peptidoglycan contains pentapeptides that are trimmed by
carboxypeptidases to tetra- and tripeptides. The well-characterized
DD-carboxypeptidases hydrolyze the terminal D-alanine from the stem pentapeptide
to produce a tetrapeptide. However, few LD-carboxypeptidases that produce
tripeptides have been identified, and nothing is known about substrate
specificity in these enzymes. We report biochemical properties and crystal
structures of the LD-carboxypeptidases LdcB from Streptococcus pneumoniae,
Bacillus anthracis, and Bacillus subtilis. The enzymes are active against
bacterial cell wall tetrapeptides and adopt a zinc-carboxypeptidase fold
characteristic of the LAS superfamily. We have also solved the structure of
S. pneumoniae LdcB with a product mimic, elucidating the residues essential for
peptidoglycan recognition and the conformational changes that occur on ligand
binding.
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