1m5s

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[[Image:1m5s.jpg|left|200px]]
 
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{{Structure
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==Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri==
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|PDB= 1m5s |SIZE=350|CAPTION= <scene name='initialview01'>1m5s</scene>, resolution 1.85&Aring;
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<StructureSection load='1m5s' size='340' side='right'caption='[[1m5s]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1m5s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5S FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 1.85&#8491;</td></tr>
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|GENE=
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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=1m5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5s OCA], [https://pdbe.org/1m5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5s RCSB], [https://www.ebi.ac.uk/pdbsum/1m5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5s ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri'''
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[https://www.uniprot.org/uniprot/FTR_METBF FTR_METBF] 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).
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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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Formyltransferase catalyzes the reversible formation of formylmethanofuran from N(5)-formyltetrahydromethanopterin and methanofuran, a reaction involved in the C1 metabolism of methanogenic and sulfate-reducing archaea. The crystal structure of the homotetrameric enzyme from Methanopyrus kandleri (growth temperature optimum 98 degrees C) has recently been solved at 1.65 A resolution. We report here the crystal structures of the formyltransferase from Methanosarcina barkeri (growth temperature optimum 37 degrees C) and from Archaeoglobus fulgidus (growth temperature optimum 83 degrees C) at 1.9 A and 2.0 A resolution, respectively. Comparison of the structures of the three enzymes revealed very similar folds. The most striking difference found was the negative surface charge, which was -32 for the M. kandleri enzyme, only -8 for the M. barkeri enzyme, and -11 for the A. fulgidus enzyme. The hydrophobic surface fraction was 50% for the M. kandleri enzyme, 56% for the M. barkeri enzyme, and 57% for the A. fulgidus enzyme. These differences most likely reflect the adaptation of the enzyme to different cytoplasmic concentrations of potassium cyclic 2,3-diphosphoglycerate, which are very high in M. kandleri (&gt;1 M) and relatively low in M. barkeri and A. fulgidus. Formyltransferase is in a monomer/dimer/tetramer equilibrium that is dependent on the salt concentration. Only the dimers and tetramers are active, and only the tetramers are thermostable. The enzyme from M. kandleri is a tetramer, which is active and thermostable only at high concentrations of potassium phosphate (&gt;1 M) or potassium cyclic 2,3-diphosphoglycerate. Conversely, the enzyme from M. barkeri and A. fulgidus already showed these properties, activity and stability, at much lower concentrations of these strong salting-out salts.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/1m5s_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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1M5S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5S 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=1m5s ConSurf].
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Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship., Mamat B, Roth A, Grimm C, Ermler U, Tziatzios C, Schubert D, Thauer RK, Shima S, Protein Sci. 2002 Sep;11(9):2168-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12192072 12192072]
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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: Methanosarcina barkeri]]
[[Category: Methanosarcina barkeri]]
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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: Grimm C]]
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[[Category: Grimm, C.]]
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[[Category: Mamat B]]
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[[Category: Mamat, B.]]
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[[Category: Roth A]]
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[[Category: Roth, A.]]
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[[Category: Schubert D]]
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[[Category: Schubert, D.]]
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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: Tziatzios C]]
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[[Category: Tziatzios, C.]]
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[[Category: alpha/beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:14 2008''
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Current revision

Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri

PDB ID 1m5s

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