Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase

Anne Roberts; Jeffrey G Pelton; David E Wemmer

doi:10.1002/mrc.1823

Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase

Magn Reson Chem. 2006 Jul:44 Spec No:S71-82. doi: 10.1002/mrc.1823.

Authors

Anne Roberts¹, Jeffrey G Pelton, David E Wemmer

Affiliation

¹ Department of Chemistry, University of California and Physical Biosciences Division, Lawrence Berkeley National Lab, Berkeley, CA 94720-1460, USA.

PMID: 16826543
DOI: 10.1002/mrc.1823

Abstract

The structure of an O6-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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Methanococcus / enzymology*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
O(6)-Methylguanine-DNA Methyltransferase / chemistry*
Protein Conformation
Protein Structure, Tertiary

Substances

O(6)-Methylguanine-DNA Methyltransferase