1m5s: Difference between revisions

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<StructureSection load='1m5s' size='340' side='right'caption='[[1m5s]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1m5s' size='340' side='right'caption='[[1m5s]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m5s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"methanosarcina_barkerii"_(sic)_schnellen_1947 "methanosarcina barkerii" (sic) schnellen 1947]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M5S FirstGlance]. <br>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ftr|1ftr]], [[1m5h|1m5h]]</td></tr>
</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5s OCA], [http://pdbe.org/1m5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m5s RCSB], [http://www.ebi.ac.uk/pdbsum/1m5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:12192072<ref>PMID:12192072</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1m5s" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Formylmethanofuran--tetrahydromethanopterin N-formyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ermler, U]]
[[Category: Methanosarcina barkeri]]
[[Category: Grimm, C]]
[[Category: Ermler U]]
[[Category: Mamat, B]]
[[Category: Grimm C]]
[[Category: Roth, A]]
[[Category: Mamat B]]
[[Category: Schubert, D]]
[[Category: Roth A]]
[[Category: Shima, S]]
[[Category: Schubert D]]
[[Category: Thauer, R K]]
[[Category: Shima S]]
[[Category: Tziatzios, C]]
[[Category: Thauer RK]]
[[Category: Alpha/beta sandwich]]
[[Category: Tziatzios C]]
[[Category: Transferase]]
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