1M5H

Formylmethanofuran:tetrahydromethanopterin formyltransferase from Archaeoglobus fulgidus

Summary for 1M5H

• Entry DOI: 10.2210/pdb1m5h/pdb
• Related: 1FTR 1M5S
• Descriptor: Formylmethanofuran--tetrahydromethanopterin formyltransferase, POTASSIUM ION (3 entities in total)
• Functional Keywords: alpha/beta sandwich, transferase
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cytoplasm (By similarity): O28076
• Total number of polymer chains: 8
• Total formula weight: 254555.86

Authors

Mamat, B.,Roth, A.,Grimm, C.,Ermler, U.,Tziatzios, C.,Schubert, D.,Thauer, R.K.,Shima, S. (deposition date: 2002-07-09, release date: 2002-07-26, Last modification date: 2024-04-03)

Primary citation

Mamat, B.,Roth, A.,Grimm, C.,Ermler, U.,Tziatzios, C.,Schubert, D.,Thauer, R.K.,Shima, S.
Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.
Protein Sci., 11:2168-2178, 2002

PubMed Abstract: 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.

PubMed: 12192072
DOI: 10.1110/ps.0211002

Experimental method

X-RAY DIFFRACTION (2 Å)