Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase
Journal Article
·
· Magnetic Resonance in Chemistry
OSTI ID:891630
The structure of an O{sub 6}-methylguanine methyltransferase from the thermophile Methanococcus jannaschii has been determined using multinuclear multidimensional NMR spectroscopy. The structure is similar to homologues 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.
- Research Organization:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE Director. Office of Science. Office of Biological andEnvironmental Research; National Science Foundation Grants DMB 8609035and BBS8720134
- DOE Contract Number:
- DE-AC02-05CH11231
- OSTI ID:
- 891630
- Report Number(s):
- LBNL-59310; MRCHEG; R&D Project: GTL2KW; BnR: KP1102010; TRN: US200622%%272
- Journal Information:
- Magnetic Resonance in Chemistry, Vol. 44, Issue SI; Related Information: Journal Publication Date: 07/2006; ISSN 0749-1581
- Country of Publication:
- United States
- Language:
- English
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