1fmt

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(New page: 200px<br /><applet load="1fmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmt, resolution 2.0&Aring;" /> '''METHIONYL-TRNAFMET FO...)
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[[Image:1fmt.gif|left|200px]]<br /><applet load="1fmt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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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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==Overview==
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==METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI==
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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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<StructureSection load='1fmt' size='340' side='right'caption='[[1fmt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fmt]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMT FirstGlance]. <br>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FMT OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmt OCA], [https://pdbe.org/1fmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmt RCSB], [https://www.ebi.ac.uk/pdbsum/1fmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmt ProSAT]</span></td></tr>
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==Reference==
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</table>
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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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== Function ==
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[https://www.uniprot.org/uniprot/FMT_ECOLI FMT_ECOLI] Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fmt ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Methionyl-tRNA formyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Mechulam Y]]
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[[Category: Mechulam, Y.]]
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[[Category: Schmitt E]]
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[[Category: Schmitt, E.]]
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[[Category: formyltransferase]]
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[[Category: initiator trna]]
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[[Category: translation initiation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:02:49 2007''
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Current revision

METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI

PDB ID 1fmt

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