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  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., et al. (2002). Crystal structures and enzymatic properties of three formyltransferases from archaea: Environmental adaptation and evolutionary relationship. Protein Science, 11(9), 2168-2178.

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Mamat, B., Autor
Roth, A., Autor
Grimm, C.1, Autor           
Ermler, U., Autor
Tziatzios, C., Autor
Schubert, D., Autor
Thauer, R. K.2, Autor           
Shima, S.3, Autor           
Affiliations:
1Department of Organismic Interactions, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266313              
2Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266289              
3Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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Schlagwörter: formyltransferase; crystal structure; monomer/dimer/tetramer association equilibrium; Methanosarcina barkeri; Methanopyrus kandleri; Archaeoglobus fulgidus; methanogenic archaea; sulfate-reducing archaea
 Zusammenfassung: Formyltransferase catalyzes the reversible formation of formylmethanofuran from N5-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 98degreesC) has recently been solved at 1.65 Angstrom resolution. We report here the crystal structures of the formyltransferase from Methanosarcina barkeri (growth temperature optimum 37degreesC) and from Archaeoglobus fulgidus (growth temperature optimum 83degreesC) at 1.9 Angstrom and 2.0 Angstrom 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. [References: 49]

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Sprache(n): eng - English
 Datum: 2002-09
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 13924
ISI: 000177558400010
 Art des Abschluß: -

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Titel: Protein Science
  Alternativer Titel : Protein Sci.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 11 (9) Artikelnummer: - Start- / Endseite: 2168 - 2178 Identifikator: ISSN: 0961-8368