1fmt

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[[Image:1fmt.gif|left|200px]]<br /><applet load="1fmt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fmt.gif|left|200px]]
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caption="1fmt, resolution 2.0&Aring;" />
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'''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1fmt |SIZE=350|CAPTION= <scene name='initialview01'>1fmt</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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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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'''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMT OCA].
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1FMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8887566 8887566]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8887566 8887566]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionyl-tRNA formyltransferase]]
[[Category: Methionyl-tRNA formyltransferase]]
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[[Category: translation initiation]]
[[Category: translation initiation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:09 2008''

Revision as of 09:11, 20 March 2008


PDB ID 1fmt

Drag the structure with the mouse to rotate
, resolution 2.0Å
Gene: FMT (Escherichia coli)
Activity: Methionyl-tRNA formyltransferase, with EC number 2.1.2.9
Coordinates: save as pdb, mmCIF, xml



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

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