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His84 rather than His35 is the active site histidine in the corrinoid protein MtrA of the energy conserving methyltransferase complex from Methanobacterium thermoautotrophicum

MPS-Authors

Sauer,  Karin
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Thauer,  Rudolf K.       
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Citation

Sauer, K., & Thauer, R. K. (1998). His84 rather than His35 is the active site histidine in the corrinoid protein MtrA of the energy conserving methyltransferase complex from Methanobacterium thermoautotrophicum. FEBS Letters, 436(3), 401-402. doi:10.1016/S0014-5793(98)01180-6.


Cite as: https://hdl.handle.net/21.11116/0000-000F-ADBE-9
Abstract
The energy conserving corrinoid containing MtrA-H complex from
Methanobacterium thermoautotrophicum is composed of eight different
subunits of which MtrA harbors the corrinoid prosthetic group, the
corrinoid being bound in the base-off/His-on configuration. Based on
sequence comparisons it was recently proposed that His(35) Of MtrA is
the active site histidine, We report here that His(84) rather than
His(35) is the axial ligand to the cobamide in MtrA, (C) 1998 Federation
of European Biochemical Societies.