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1m5s

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[[Image:1m5s.jpg|left|200px]]
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{{STRUCTURE_1m5s| PDB=1m5s | SCENE= }}
{{STRUCTURE_1m5s| PDB=1m5s | SCENE= }}
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'''Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri'''
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===Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri===
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==Overview==
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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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{{ABSTRACT_PUBMED_12192072}}
==About this Structure==
==About this Structure==
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[[Category: Tziatzios, C.]]
[[Category: Tziatzios, C.]]
[[Category: Alpha/beta sandwich]]
[[Category: Alpha/beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:40:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:16:25 2008''

Revision as of 20:16, 2 July 2008

Image:1m5s.png

Template:STRUCTURE 1m5s

Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri

Template:ABSTRACT PUBMED 12192072

About this Structure

1M5S is a Single protein structure of sequence from Methanosarcina barkeri. 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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