E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form-Reference-Cited by-同舟云学术

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E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form

Published:2018-08-11 Issue:16 Volume:46 Page:8641-8650
ISSN:0305-1048
Container-title:Nucleic Acids Research
language:en
Short-container-title:

Author:

Johansen Jesper S¹,Kavaliauskas Darius¹,Pfeil Shawn H²,Blaise Mickaël¹,Cooperman Barry S³,Goldman Yale E⁴,Thirup Søren S¹,Knudsen Charlotte R¹^ORCID

Affiliation:

1. Department of Molecular Biology & Genetics, University of Aarhus, Gustav Wieds Vej 10 C, DK-8000 Aarhus C, Denmark

2. Department of Physics, West Chester University, West Chester, PA 19383, USA

3. Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA

4. Pennsylvania Muscle Institute, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA

Funder

National Institutes of Health

Publisher

Oxford University Press (OUP)

Subject

Genetics

Link

http://academic.oup.com/nar/article-pdf/46/16/8641/25802496/gky697.pdf

Reference59 articles.

1. The P-loop - a common motif in ATP-and GTP-binding proteins;Sareste;Trends Biochem. Sci.,1990

2. The GTPase superfamily: conserved structure and molecular mechanism;Bourne;Nature,1991

3. The GTP binding motif: variations on a theme;Kjeldgaard;FASEB J.,1996

4. Structure-function relationships of the G domain, a canonical switch motif;Wittinghofer;Annu. Rev. Biochem.,2011

5. Cofactor dependent conformational switching of GTPases;Hauryliuk;Biophys. J.,2008

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