1fmt

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[[Image:1fmt.gif|left|200px]]
[[Image:1fmt.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1fmt |SIZE=350|CAPTION= <scene name='initialview01'>1fmt</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1fmt", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl-tRNA_formyltransferase Methionyl-tRNA formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.9 2.1.2.9] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= FMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1fmt| PDB=1fmt | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmt OCA], [http://www.ebi.ac.uk/pdbsum/1fmt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fmt RCSB]</span>
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}}
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'''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''
'''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''
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[[Category: Mechulam, Y.]]
[[Category: Mechulam, Y.]]
[[Category: Schmitt, E.]]
[[Category: Schmitt, E.]]
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[[Category: formyltransferase]]
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[[Category: Formyltransferase]]
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[[Category: initiator trna]]
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[[Category: Initiator trna]]
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[[Category: translation initiation]]
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[[Category: Translation initiation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:30:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:02 2008''
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Revision as of 13:30, 2 May 2008

Image:1fmt.gif

Template:STRUCTURE 1fmt

METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI


Overview

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.

About this Structure

1FMT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase., Schmitt E, Blanquet S, Mechulam Y, EMBO J. 1996 Sep 2;15(17):4749-58. PMID:8887566 Page seeded by OCA on Fri May 2 16:30:53 2008

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