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PDBsum entry 2exb
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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 structure of penicillin binding protein 4 (dacb) from escherichia coli, Both in the native form and covalently linked to various antibiotics.
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Authors
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H.Kishida,
S.Unzai,
D.I.Roper,
A.Lloyd,
S.Y.Park,
J.R.Tame.
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Ref.
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Biochemistry, 2006,
45,
783-792.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia
coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is
presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in
the synthesis and maintenance of the cell wall. The model contains a penicillin
binding domain similar to known structures, but includes a large insertion which
folds into domains with unique folds. The structures of the protein covalently
attached to five different antibiotics presented here show the active site
residues are unmoved compared to the apoprotein, but nearby surface loops and
helices are displaced in some cases. The altered geometry of conserved active
site residues compared with those of other PBPs suggests a possible cause for
the slow deacylation rate of PBP4.
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