1ftr

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(New page: 200px<br /><applet load="1ftr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ftr, resolution 1.7&Aring;" /> '''FORMYLMETHANOFURAN:TE...)
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[[Image:1ftr.jpg|left|200px]]<br /><applet load="1ftr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ftr, resolution 1.7&Aring;" />
 
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'''FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI'''<br />
 
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==Overview==
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==FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI==
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BACKGROUND: Formylmethanofuran: tetrahydromethanopterin formyltransferase, (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth, temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely, dependent on the presence of lyotropic salts for activity and, thermostability. The enzyme is involved in the pathway of carbon dioxide, reduction to methane and catalyzes the transfer of formyl from, formylmethanofuran to tetrahydromethanopterin. RESULTS: The crystal, structure of Ftr, determined to a resolution of 1:73 AE reveals a, homotetramer composed essentially of two dimers. Each subunit is, subdivided into two tightly associated lobes both consisting of a, predominantly antiparallel beta sheet flanked by alpha helices forming an, alpha/beta sandwich structure. The approximate location of the active site, was detected in a region close to the dimer interface. CONCLUSIONS: The, adaptation of Ftr against high lyotropic salt concentrations is, structurally reflected by a large number of negatively charged residues, and their high local concentration on the surface of the protein. The, salt-dependent thermostability of Ftr might be explained on a molecular, basis by ionic interactions at the protein surface, involving both protein, and inorganic salt ions, and the mainly hydrophobic interactions between, the subunits and within the core.
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<StructureSection load='1ftr' size='340' side='right'caption='[[1ftr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ftr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FTR FirstGlance]. <br>
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1FTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Active as [http://en.wikipedia.org/wiki/Formylmethanofuran--tetrahydromethanopterin_N-formyltransferase Formylmethanofuran--tetrahydromethanopterin N-formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.101 2.3.1.101] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FTR 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]] 1.7&#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=1ftr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ftr OCA], [https://pdbe.org/1ftr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ftr RCSB], [https://www.ebi.ac.uk/pdbsum/1ftr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ftr ProSAT]</span></td></tr>
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==Reference==
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</table>
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Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability., Ermler U, Merckel M, Thauer R, Shima S, Structure. 1997 May 15;5(5):635-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9195883 9195883]
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== Function ==
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[[Category: Formylmethanofuran--tetrahydromethanopterin N-formyltransferase]]
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[https://www.uniprot.org/uniprot/FTR_METKA FTR_METKA] Catalyzes the reversible transfer of a formyl group from formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) so as to produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and methanofuran (MFR).[HAMAP-Rule:MF_00579]
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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/ft/1ftr_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=1ftr ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanopyrus kandleri]]
[[Category: Methanopyrus kandleri]]
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[[Category: Single protein]]
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[[Category: Ermler U]]
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[[Category: Ermler, U.]]
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[[Category: Merckel MC]]
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[[Category: Merckel, M.C.]]
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[[Category: Shima S]]
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[[Category: Shima, S.]]
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[[Category: Thauer RK]]
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[[Category: Thauer, R.K.]]
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[[Category: acyltransferase]]
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[[Category: archae]]
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[[Category: formyltransferase]]
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[[Category: halophilic]]
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[[Category: hyperthermophilic]]
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[[Category: methanogenesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:16:30 2007''
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Current revision

FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI

PDB ID 1ftr

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