1ftr

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[[Image:1ftr.jpg|left|200px]]
 
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==FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI==
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The line below this paragraph, containing "STRUCTURE_1ftr", creates the "Structure Box" on the page.
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<StructureSection load='1ftr' size='340' side='right'caption='[[1ftr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1ftr| PDB=1ftr | SCENE= }}
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</table>
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== Function ==
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'''FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI'''
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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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==Overview==
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Check<jmol>
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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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<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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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1FTR is a [[Single protein]] structure of sequence from [http://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].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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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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://www.ncbi.nlm.nih.gov/pubmed/9195883 9195883]
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<div style="clear:both"></div>
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[[Category: Formylmethanofuran--tetrahydromethanopterin N-formyltransferase]]
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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://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:45:25 2008''
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Current revision

FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI

PDB ID 1ftr

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