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PDBsum entry 1mla
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Acyltransferase
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PDB id
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1mla
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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 escherichia coli malonyl-Coa:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
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Authors
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L.Serre,
E.C.Verbree,
Z.Dauter,
A.R.Stuitje,
Z.S.Derewenda.
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Ref.
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J Biol Chem, 1995,
270,
12961-12964.
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PubMed id
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Abstract
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Endogenous fatty acids are synthesized in all organisms in a pathway catalyzed
by the fatty acid synthase complex. In bacteria, where the fatty acids are used
primarily for incorporation into components of cell membranes, fatty acid
synthase is made up of several independent cytoplasmic enzymes, each catalyzing
one specific reaction. The initiation of the elongation step, which extends the
length of the growing acyl chain by two carbons, requires the transfer of the
malonyl moiety from malonyl-CoA onto the acyl carrier protein. We report here
the crystal structure (refined at 1.5-A resolution to an R factor of 0.19) of
the malonyl-CoA specific transferase from Escherichia coli. The protein has an
alpha/beta type architecture, but its fold is unique. The active site inferred
from the location of the catalytic Ser-92 contains a typical nucleophilic elbow
as observed in alpha/beta hydrolases. Serine 92 is hydrogen bonded to His-201 in
a fashion similar to various serine hydrolases. However, instead of a carboxyl
acid typically found in catalytic triads, the main chain carbonyl of Gln-250
serves as a hydrogen bond acceptor in an interaction with His-201. Two other
residues, Arg-117 and Glu-11, are also located in the active site, although
their function is not clear.
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