HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 7, 4261-4266, February 17, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/7/4261    most recent M511567200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lee, H. H. Articles by Suh, S. W. Search for Related Content PubMed PubMed Citation Articles by Lee, H. H. Articles by Suh, S. W. Social Bookmarking                      What's this?

Crystal Structure of a Metal Ion-bound IS200 Transposase^*

Hyung Ho Lee¹, Ji Young Yoon¹, Hyoun Sook Kim¹, Ji Yong Kang¹, Kyoung Hoon Kim¹, Do Jin Kim¹, Jun Yong Ha¹, Bunzo Mikami, Hye Jin Yoon, and Se Won Suh²

From the Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea and Laboratory of Quality Design and Exploitation, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan

IS200 transposases, present in many bacteria and Archaea, appear to be distinct from other groups of transposases. To provide a structural basis for understanding the action of IS200 transposases, we have determined the crystal structure of the SSO1474 protein from Sulfolobus solfataricus, a member of the IS200 family, in both Mn²⁺-bound and Mn²⁺-free forms. Its monomer fold is distinct from other classes of structurally characterized transposases. Two monomers form a tight dimer by exchanging the C-terminal -helix and by merging the two central -sheets into a large -sheet. Glu⁵⁵, His⁶², and four water molecules provide the direct coordination sphere of the catalytically essential metal ion in the Mn²⁺-bound structure. His¹⁶, Asp⁵⁹, and His⁶⁰ also play important roles in maintaining the metal binding site. The catalytic site is formed at the interface between monomers. The candidate nucleophile in the transposition mechanism, strictly conserved Tyr¹²¹ coming from the other monomer, is turned away from the active site, suggesting that a conformational change is likely to occur during the catalytic cycle.

Received for publication, October 25, 2005 , and in revised form, November 14, 2005.

The atomic coordinates and structure factors (code 2F4F and 2F5G) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by a grant from the Korea Ministry of Science and Technology (NRL-2001). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental data and Figs. S1–S4.

¹ Recipients of the BK21 fellowship of the Korean Ministry of Education.

² To whom correspondence should be addressed. Tel.: 82-2-880-6653; Fax: 82-2-889-1568; E-mail: sewonsuh{at}snu.ac.kr.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Filee, P. Siguier, and M. Chandler Insertion Sequence Diversity in Archaea Microbiol. Mol. Biol. Rev., March 1, 2007; 71(1): 121 - 157. [Abstract] [Full Text] [PDF]