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PDBsum entry 2wok
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Peptide binding protein/peptide
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PDB id
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2wok
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References listed in PDB file
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Key reference
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Title
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Crystal structures of an oligopeptide-Binding protein from the biosynthetic pathway of the beta-Lactamase inhibitor clavulanic acid.
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Authors
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A.K.Mackenzie,
K.Valegård,
A.Iqbal,
M.E.Caines,
N.J.Kershaw,
S.E.Jensen,
C.J.Schofield,
I.Andersson.
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Ref.
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J Mol Biol, 2010,
396,
332-344.
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PubMed id
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Abstract
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Clavulanic acid (CA) is a clinically important beta-lactamase inhibitor that is
produced by fermentation of Streptomyces clavuligerus. The CA biosynthesis
pathway starts from arginine and glyceraldehyde-3-phosphate and proceeds via
(3S,5S)-clavaminic acid, which is converted to (3R,5R)-clavaldehyde, the
immediate precursor of (3R,5R)-CA. Open reading frames 7 (orf7) and 15 (orf15)
of the CA biosynthesis cluster encode oligopeptide-binding proteins (OppA1 and
OppA2), which are essential for CA biosynthesis. OppA1/2 are proposed to be
involved in the binding and/or transport of peptides across the S. clavuligerus
cell membrane. Peptide binding assays reveal that recombinant OppA1 and OppA2
bind di-/tripeptides containing arginine and certain nonapeptides including
bradykinin. Crystal structures of OppA2 in its apo form and in complex with
arginine or bradykinin were solved to 1.45, 1.7, and 1.7 A resolution,
respectively. The overall fold of OppA2 consists of two lobes with a deep cavity
in the center, as observed for other oligopeptide-binding proteins. The large
cavity creates a peptide/arginine binding cleft. The crystal structures of OppA2
in complex with arginine or bradykinin reveal that the C-terminal arginine of
bradykinin binds similarly to arginine. The results are discussed in terms of
the possible roles of OppA1/2 in CA biosynthesis.
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