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Title: Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase

Abstract

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.

Authors:
; ;
Publication Date:
Research Org.:
Ernest Orlando Lawrence Berkeley NationalLaboratory, Berkeley, CA (US)
Sponsoring Org.:
USDOE Director. Office of Science. Office of Biological andEnvironmental Research; National Science Foundation Grants DMB 8609035and BBS8720134
OSTI Identifier:
891630
Report Number(s):
LBNL-59310
Journal ID: ISSN 0749-1581; MRCHEG; R&D Project: GTL2KW; BnR: KP1102010; TRN: US200622%%272
DOE Contract Number:  
DE-AC02-05CH11231
Resource Type:
Journal Article
Resource Relation:
Journal Name: Magnetic Resonance in Chemistry; Journal Volume: 44; Journal Issue: SI; Related Information: Journal Publication Date: 07/2006
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; CRYSTALLOGRAPHY; FLEXIBILITY; PROTEINS; SPECTROSCOPY; NMR protein structure DNA Methyltransferase DNA repair

Citation Formats

Roberts, Anne, Pelton, Jeffrey G., and Wemmer, David E. Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase. United States: N. p., 2006. Web.
Roberts, Anne, Pelton, Jeffrey G., & Wemmer, David E. Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase. United States.
Roberts, Anne, Pelton, Jeffrey G., and Wemmer, David E. Tue . "Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase". United States. doi:. https://www.osti.gov/servlets/purl/891630.
@article{osti_891630,
title = {Structural Studies of MJ1529, an O6-methylguanine-DNAMethyltransferase},
author = {Roberts, Anne and Pelton, Jeffrey G. and Wemmer, David E.},
abstractNote = {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.},
doi = {},
journal = {Magnetic Resonance in Chemistry},
number = SI,
volume = 44,
place = {United States},
year = {Tue Jan 10 00:00:00 EST 2006},
month = {Tue Jan 10 00:00:00 EST 2006}
}