1m5h
From Proteopedia
(New page: 200px<br /><applet load="1m5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5h, resolution 2.00Å" /> '''Formylmethanofuran:t...) |
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| - | [[Image:1m5h.gif|left|200px]]<br /><applet load="1m5h" size=" | + | [[Image:1m5h.gif|left|200px]]<br /><applet load="1m5h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m5h, resolution 2.00Å" /> | caption="1m5h, resolution 2.00Å" /> | ||
'''Formylmethanofuran:tetrahydromethanopterin formyltransferase from Archaeoglobus fulgidus'''<br /> | '''Formylmethanofuran:tetrahydromethanopterin formyltransferase from Archaeoglobus fulgidus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Formyltransferase catalyzes the reversible formation of formylmethanofuran | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1M5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1M5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1M5H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schubert, D.]] | [[Category: Schubert, D.]] | ||
[[Category: Shima, S.]] | [[Category: Shima, S.]] | ||
| - | [[Category: Thauer, R | + | [[Category: Thauer, R K.]] |
[[Category: Tziatzios, C.]] | [[Category: Tziatzios, C.]] | ||
[[Category: K]] | [[Category: K]] | ||
[[Category: alpha/beta sandwich]] | [[Category: alpha/beta sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:39 2008'' |
Revision as of 11:51, 21 February 2008
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Formylmethanofuran:tetrahydromethanopterin formyltransferase from Archaeoglobus fulgidus
Overview
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.
About this Structure
1M5H is a Single protein structure of sequence from Archaeoglobus fulgidus with as ligand. Active as Formylmethanofuran--tetrahydromethanopterin N-formyltransferase, with EC number 2.3.1.101 Full crystallographic information is available from OCA.
Reference
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
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