Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Protein Science (2004), 13:659-667. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gutiérrez, P.
Right arrow Articles by Gehring, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gutiérrez, P.
Right arrow Articles by Gehring, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Structure of the archaeal translation initiation factor aIF2{beta} from Methanobacterium thermoautotrophicum: Implications for translation initiation

Pablo Gutiérrez1,4, Michael J. Osborne1,4, Nadeem Siddiqui1,4, Jean-François Trempe1,4, Cheryl Arrowsmith2,3 and Kalle Gehring1,4

1 McGill University, Department of Biochemistry, McIntyre Medical Science Building, Montréal, Québec H3G 1Y6, Canada
2 Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada
3 Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada
4 Montreal Joint Centre for Structural Biology, Montréal, Québec, Canada

(RECEIVED November 4, 2003; FINAL REVISION December 1, 2003; ACCEPTED December 1, 2003)



Abstract

aIF2{beta} is the archaeal homolog of eIF2{beta}, a member of the eIF2 heterotrimeric complex, implicated in the delivery of Met-tRNAiMet to the 40S ribosomal subunit. We have determined the solution structure of the intact {beta}-subunit of aIF2 from Methanobacterium thermoautotrophicum. aIF2{beta} is composed of an unfolded N terminus, a mixed {alpha}/{beta} core domain and a C-terminal zinc finger. NMR data shows the two folded domains display restricted mobility with respect to each other. Analysis of the aIF2{gamma} structure docked to tRNA allowed the identification of a putative binding site for the {beta}-subunit in the ternary translation complex. Based on structural similarity and biochemical data, a role for the different secondary structure elements is suggested.

Keywords: aIF2{beta}; translation initiation; archaebacteria; NMR

Reprint requests to: Kalle Gehring, McGill University, Department of Biochemistry, McIntyre Medical Science Building, 3655 Promenade Sir William Osler, Montréal, Québec H3G 1Y6, Canada; e-mail: Kalle. Gehring{at}mcgill.ca; fax: (514) 398-7384.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03506604.


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


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Yatime, Y. Mechulam, S. Blanquet, and E. Schmitt
Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
PNAS, November 20, 2007; 104(47): 18445 - 18450.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. Sokabe, M. Yao, N. Sakai, S. Toya, and I. Tanaka
Structure of archaeal translational initiation factor 2 beta{gamma}-GDP reveals significant conformational change of the beta-subunit and switch 1 region
PNAS, August 29, 2006; 103(35): 13016 - 13021.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.