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Structural studies of MJ1529, an O 6 ‐methylguanine‐DNA methyltransferase
Author(s) -
Roberts Anne,
Pelton Jeffrey G.,
Wemmer David E.
Publication year - 2006
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1823
Subject(s) - chemistry , methyltransferase , dna methyltransferase , methanococcus , dna , nuclear magnetic resonance spectroscopy , sequence (biology) , thermophile , function (biology) , stereochemistry , domain (mathematical analysis) , crystallography , biochemistry , enzyme , archaea , genetics , gene , methylation , biology , mathematical analysis , mathematics
The structure of an O 6 ‐methylguanine‐DNA methyltransferase (MGMT) from the thermophile Methanococcus jannaschii has been determined using multinuclear multidimensional NMR spectroscopy. The structure is similar to homologs from other organisms that have been determined by crystallography, with some variation in the N ‐terminal domain. The C ‐terminal domain is more highly conserved in both sequence and structure. Regions of the protein show broadening, reflecting conformational flexibility that is likely related to function. Copyright © 2006 John Wiley & Sons, Ltd.