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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. doi:10.1110/ps.0211002.

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 Creators:
Mamat, Björn1, 2, 3, Author           
Roth, Annette1, Author           
Grimm, Clemens1, Author           
Ermler, Ulrich1, Author           
Tziatzios, Christos4, Author
Schubert, Dieter4, Author
Thauer, Rudolf Kurt2, Author           
Shima, Seigo2, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3135468              
3Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, 35043 Marburg, Germany, ou_persistent22              
4Institut für Biophysik der Johann Wolfgang Goethe-Universität, 60590 Frankfurt am Main, Germany , ou_persistent22              

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Free keywords: Formyltransferase; Crystal structure; Monomer/dimer/tetramer association equilibrium; Methanosarcina barkeri; Methanopyrus kandleri; Archaeoglobus fulgidus; Methanogenic archaea; Sulfate-reducing archaea; Hyperthermophilic methanopyrus-kandleri; Tetrahydromethanopterin formyltransferase; Archaeoglobus-fulgidus; Sp-nov; Association equilibrium; Methanosarcina-barkeri; Molecular replacement; Salt-dependence; Formylmethanofuran
 Abstract: 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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Language(s): eng - English
 Dates: 2002-06-062002-05-152002-06-182002-09
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1110/ps.0211002
PMID: 12192072
PMC: PMC2373594
 Degree: -

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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 11 (9) Sequence Number: - Start / End Page: 2168 - 2178 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760