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His 84 rather than His 35 is the active site histidine in the corrinoid protein MtrA of the energy conserving methyltransferase complex from Methanobacterium thermoautotrophicum
Author(s) -
Sauer Karin,
Thauer Rudolf K
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01180-6
Subject(s) - corrinoid , chemistry , histidine , methyltransferase , active site , methanobacterium , stereochemistry , methylation , biochemistry , enzyme , dna , archaea , gene
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.