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PDBsum entry 1qwz
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of sortase b, A cysteine transpeptidase that tethers surface protein to the staphylococcus aureus cell wall.
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Authors
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Y.Zong,
S.K.Mazmanian,
O.Schneewind,
S.V.Narayana.
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Ref.
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Structure, 2004,
12,
105-112.
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PubMed id
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Abstract
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Many surface proteins of Gram-positive bacteria, which play important roles
during the pathogenesis of human infections, are anchored to the cell wall
envelope by a mechanism requiring sortases. Sortase B, a cysteine transpeptidase
from Staphylococcus aureus, cleaves the C-terminal sorting signal of IsdC at the
NPQTN motif and tethers the polypeptide to the pentaglycine cell wall
cross-bridge. During catalysis, the active site cysteine of sortase and the
cleaved substrate form an acyl intermediate, which is then resolved by the amino
group of pentaglycine cross-bridges. We report here the crystal structures of
SrtBDeltaN30 in complex with two active site inhibitors, MTSET and E64, and with
the cell wall substrate analog tripleglycine. These structures reveal, for the
first time, the active site disposition and the unique Cys-Arg catalytic
machinery of the cysteine transpeptidase, and they also provide useful
information for the future design of anti-infective agents against sortases.
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