Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (802K) Freely available
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 ISI Web of Science
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 (38)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Grazulis, S.
Right arrow Articles by Siksnys, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grazulis, S.
Right arrow Articles by Siksnys, V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2002, Vol. 30, No. 4 876-885
© 2002 Oxford University Press

Crystal structure of the Bse634I restriction endonuclease: comparison of two enzymes recognizing the same DNA sequence

Saulius Grazulis1,2,*, Markus Deibert1, Renata Rimseliene2, Remigijus Skirgaila2, Giedrius Sasnauskas2, Arunas Lagunavicius2, Vladimir Repin3, Claus Urbanke4, Robert Huber1 and Virginijus Siksnys2

1Max-Planck Institut für Biochemie, Abt. Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried (bei München), Germany, 2Institute of Biotechnology, Graiciuno 8, LT-2028 Vilnius, Lithuania, 3State Research Center of Virology and Biotechnology ‘Vector’, Koltsovo, Novosibirsk region, 630559, Russia and 4Abteilung für Biophysikalisch-biochemische Verfahren, Medizinische Hochschule Hannover, Carl Neuberg Strasse 1, D-30632 Hannover, Germany

Crystal structures of Type II restriction endonucleases demonstrate a conserved common core and active site residues but diverse structural elements involved in DNA sequence discrimination. Comparative structural analysis of restriction enzymes recognizing the same nucleotide sequence might therefore contribute to our understanding of the structural diversity of specificity determinants within restriction enzymes. We have solved the crystal structure of the Bacillus stearothermophilus restriction endonuclease Bse634I by the multiple isomorphous replacement technique to 2.17 Å resolution. Bse634I is an isoschisomer of the Cfr10I restriction enzyme whose crystal structure has been reported previously. Comparative structural analysis of the first pair of isoschisomeric enzymes revealed conserved structural determinants of sequence recognition and catalysis. However, conformations of the N-terminal subdomains differed between Bse634I/Cfr10I, suggesting a rigid body movement that might couple DNA recognition and catalysis. Structural similarities extend to the quaternary structure level: crystal contacts suggest that Bse634I similarly to Cfr10I is arranged as a tetramer. Kinetic analysis reveals that Bse634I is able to interact simultaneously with two recognition sites supporting the tetrameric architecture of the protein. Thus, restriction enzymes Bse634I, Cfr10I and NgoMIV, recognizing overlapping nucleotide sequences, exhibit a conserved tetrameric architecture that is of functional importance.

* To whom correspondence should be addressed at: Institute of Biotechnology, Graiciuno 8, LT-2028 Vilnius, Lithuania. Tel: +370 2 602108; Fax: +370 2 602116; Email: grazulis{at}ibt.lt Present address:Markus Deibert, CII Group GbR, Taubenstrasse 26, D-10117 Berlin, Germany


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
G. Gasiunas, G. Sasnauskas, G. Tamulaitis, C. Urbanke, D. Razaniene, and V. Siksnys
Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family
Nucleic Acids Res., February 11, 2008; 36(3): 938 - 949.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
Q. S. Xu, R. J. Roberts, and H.-C. Guo
Two crystal forms of the restriction enzyme MspI-DNA complex show the same novel structure
Protein Sci., October 1, 2005; 14(10): 2590 - 2600.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
Z. Yang, J. R. Horton, R. Maunus, G. G. Wilson, R. J. Roberts, and X. Cheng
Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI
Nucleic Acids Res., April 1, 2005; 33(6): 1892 - 1901.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Hashimoto, T. Shimizu, T. Imasaki, M. Kato, N. Shichijo, K. Kita, and M. Sato
Crystal Structures of Type II Restriction Endonuclease EcoO109I and Its Complex with Cognate DNA
J. Biol. Chem., February 18, 2005; 280(7): 5605 - 5610.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Pingoud, A. Sudina, H. Geyer, J. M. Bujnicki, R. Lurz, G. Luder, R. Morgan, E. Kubareva, and A. Pingoud
Specificity Changes in the Evolution of Type II Restriction Endonucleases: A BIOCHEMICAL AND BIOINFORMATIC ANALYSIS OF RESTRICTION ENZYMES THAT RECOGNIZE UNRELATED SEQUENCES
J. Biol. Chem., February 11, 2005; 280(6): 4289 - 4298.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
D. M. Gowers, S. R.W. Bellamy, and S. E. Halford
One recognition sequence, seven restriction enzymes, five reaction mechanisms
Nucleic Acids Res., June 29, 2004; 32(11): 3469 - 3479.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. Mucke, D. H. Kruger, and M. Reuter
Diversity of Type II restriction endonucleases that require two DNA recognition sites
Nucleic Acids Res., November 1, 2003; 31(21): 6079 - 6084.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. Fuxreiter and I. Simon
Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases
Protein Sci., August 1, 2002; 11(8): 1978 - 1983.
[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.