Skip Navigation

Nucleic Acids Research 2006 34(7):1992-2005; doi:10.1093/nar/gkl132
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (5877K) Freely available
Right arrow Screen PDF (1169K) Freely available
Right arrow Supplementary Data
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (4)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Obarska, A.
Right arrow Articles by Firman, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Obarska, A.
Right arrow Articles by Firman, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 13 April 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Structural model for the multisubunit Type IC restriction–modification DNA methyltransferase M.EcoR124I in complex with DNA

Agnieszka Obarska, Alex Blundell1, Marcin Feder, Stepánka Vejsadová1,2, Eva Sisáková2, Marie Weiserová2, Janusz M. Bujnicki and Keith Firman1,*

Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology Trojdena 4, 02-109 Warsaw, Poland 1 IBBS Biophysics Laboratories, School of Biological Sciences, University of Portsmouth King Henry Building, King Henry I Street, Portsmouth PO1 2DY, UK 2 Institute of Microbiology, Czech Academy of Sciences Videnska 1083, 142 20 Prague 4, Czech Republic

*To whom all correspondence should be addressed. Tel: +44 2392 842059; Fax: +44 2392 842070; Email: keith.firman{at}port.ac.uk

Received November 25, 2005. Revised December 16, 2005. Accepted March 14, 2006.

Recent publication of crystal structures for the putative DNA-binding subunits (HsdS) of the functionally uncharacterized Type I restriction–modification (R-M) enzymes MjaXIP and MgeORF438 have provided a convenient structural template for analysis of the more extensively characterized members of this interesting family of multisubunit molecular motors. Here, we present a structural model of the Type IC M.EcoR124I DNA methyltransferase (MTase), comprising the HsdS subunit, two HsdM subunits, the cofactor AdoMet and the substrate DNA molecule. The structure was obtained by docking models of individual subunits generated by fold-recognition and comparative modelling, followed by optimization of inter-subunit contacts by energy minimization. The model of M.EcoR124I has allowed identification of a number of functionally important residues that appear to be involved in DNA-binding. In addition, we have mapped onto the model the location of several new mutations of the hsdS gene of M.EcoR124I that were produced by misincorporation mutagenesis within the central conserved region of hsdS, we have mapped all previously identified DNA-binding mutants of TRD2 and produced a detailed analysis of the location of surface-modifiable lysines. The model structure, together with location of the mutant residues, provides a better background on which to study protein–protein and protein–DNA interactions in Type I R-M systems.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
C. K. Kennaway, A. Obarska-Kosinska, J. H. White, I. Tuszynska, L. P. Cooper, J. M. Bujnicki, J. Trinick, and D. T. F. Dryden
The structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction protein
Nucleic Acids Res., February 1, 2009; 37(3): 762 - 770.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
J. Nakonieczna, T. Kaczorowski, A. Obarska-Kosinska, and J. M. Bujnicki
Functional Analysis of MmeI from Methanol Utilizer Methylophilus methylotrophus, a Subtype IIC Restriction-Modification Enzyme Related to Type I Enzymes
Appl. Envir. Microbiol., January 1, 2009; 75(1): 212 - 223.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
J. Youell and K. Firman
EcoR124I: from Plasmid-Encoded Restriction-Modification System to Nanodevice
Microbiol. Mol. Biol. Rev., June 1, 2008; 72(2): 365 - 377.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.