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PDBsum entry 1fmt
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Formyltransferase
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PDB id
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1fmt
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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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Structure of crystalline escherichia coli methionyl-Trna(f)met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
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Authors
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E.Schmitt,
S.Blanquet,
Y.Mechulam.
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Ref.
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Embo J, 1996,
15,
4749-4758.
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PubMed id
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Abstract
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Formylation of the methionyl moiety esterified to the 3' end of tRNA(f)Met is a
key step in the targeting of initiator tRNA towards the translation start
machinery in prokaryotes. Accordingly, the presence of methionyl-tRNA(f)Met
formyltransferase (FMT), the enzyme responsible for this formylation, is
necessary for the normal growth of Escherichia coli. The present work describes
the structure of crystalline E.coli FMT at 2.0 A, resolution. The protein has an
N-terminal domain containing a Rossmann fold. This domain closely resembles that
of the glycinamide ribonucleotide formyltransferase (GARF), an enzyme which,
like FMT, uses N-10 formyltetrahydrofolate as formyl donor. However, FMT can be
distinguished from GARF by a flexible loop inserted within its Rossmann fold. In
addition, FMT possesses a C-terminal domain with a beta-barrel reminiscent of an
OB fold. This latter domain provides a positively charged side oriented towards
the active site. Biochemical evidence is presented for the involvement of these
two idiosyncratic regions (the flexible loop in the N-terminal domain, and the
C-terminal domain) in the binding of the tRNA substrate.
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