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| [[Image:1m5s.jpg|left|200px]]<br /><applet load="1m5s" size="350" color="white" frame="true" align="right" spinBox="true"
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| caption="1m5s, resolution 1.85Å" />
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| '''Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri'''<br />
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| ==Overview== | | ==Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri== |
| 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 (>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 (>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.
| | <StructureSection load='1m5s' size='340' side='right'caption='[[1m5s]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <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> |
| 1M5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5S OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| | | <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> |
| ==Reference== | | </table> |
| 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12192072 12192072]
| | == Function == |
| [[Category: Formylmethanofuran--tetrahydromethanopterin N-formyltransferase]] | | [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). |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/1m5s_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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]. |
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Methanosarcina barkeri]] | | [[Category: Methanosarcina barkeri]] |
| [[Category: Single protein]]
| | [[Category: Ermler U]] |
| [[Category: Ermler, U.]] | | [[Category: Grimm C]] |
| [[Category: Grimm, C.]] | | [[Category: Mamat B]] |
| [[Category: Mamat, B.]] | | [[Category: Roth A]] |
| [[Category: Roth, A.]] | | [[Category: Schubert D]] |
| [[Category: Schubert, D.]] | | [[Category: Shima S]] |
| [[Category: Shima, S.]] | | [[Category: Thauer RK]] |
| [[Category: Thauer, R K.]] | | [[Category: Tziatzios C]] |
| [[Category: Tziatzios, C.]] | |
| [[Category: alpha/beta sandwich]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:49 2008''
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