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Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis.
Stuttgen, Gage M; Grosskopf, Julian D; Berger, Colton R; May, John F; Bhattacharyya, Basudeb; Weaver, Todd M.
Afiliación
  • Stuttgen GM; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
  • Grosskopf JD; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
  • Berger CR; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
  • May JF; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
  • Bhattacharyya B; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
  • Weaver TM; Department of Chemistry and Biochemistry, University Wisconsin - La Crosse, WI, USA.
FEBS Lett ; 594(2): 337-357, 2020 01.
Article en En | MEDLINE | ID: mdl-31514245
Fumarase C (FumC) catalyzes the reversible conversion of fumarate to S-malate. Previous structural investigations within the superfamily have reported a dynamic structural segment, termed the SS Loop. To date, active-site asymmetry has raised the question of how SS Loop placement affects participation of key residues during the reaction. Herein, we report structural and kinetic analyses from Escherichia coli FumC variants to understand the contribution of SS Loop residues S318, K324, and N326. High-resolution X-ray crystallographic results reveal three distinct FumC active-site conformations; disordered-open, ordered-open, and the newly discovered ordered-closed. Surprisingly, each SS Loop variant has unaffected Michaelis constants coupled to reductions in turnover number. Based upon our structural and functional analyses, we propose structural and catalytic roles for each of the aforementioned residues.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Catálisis / Fumarato Hidratasa Idioma: En Revista: FEBS Lett Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Catálisis / Fumarato Hidratasa Idioma: En Revista: FEBS Lett Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido