title: Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.
abstract: BACKGROUND
  Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The enzyme is involved in the pathway of carbon dioxide reduction to methane and catalyzes the transfer of formyl from formylmethanofuran to tetrahydromethanopterin.
  
  
  RESULTS
  The crystal structure of Ftr, determined to a resolution of 1:73 AE reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure. The approximate location of the active site was detected in a region close to the dimer interface.
  
  
  CONCLUSIONS
  The adaptation of Ftr against high lyotropic salt concentrations is structurally reflected by a large number of negatively charged residues and their high local concentration on the surface of the protein. The salt-dependent thermostability of Ftr might be explained on a molecular basis by ionic interactions at the protein surface, involving both protein and inorganic salt ions, and the mainly hydrophobic interactions between the subunits and within the core.
authors.affiliation: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Strasse 7, 60528 Frankfurt, Germany. ermler@max.mpibp.uni-frankfurt.de
authors.forename: U
authors.initials: U
authors.lastname: Ermler
authors.forename: M
authors.initials: M
authors.lastname: Merckel
authors.forename: R
authors.initials: R
authors.lastname: Thauer
authors.forename: S
authors.initials: S
authors.lastname: Shima
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D019605:Euryarchaeota / Q000201:enzymology*; D006358:Hot Temperature; D006860:Hydrogen Bonding; D019877:Hydroxymethyl and Formyl Transferases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D012492:Salts / Q000494:pharmacology; D014166:Transferases / Q000737:chemistry* / Q000187:drug effects
chemical_list: D012492:Salts; D014166:Transferases; D019877:Hydroxymethyl and Formyl Transferases; C050840:formylmethanofuran-tetrahydromethanopterin formyltransferase