Aarhus University Seal / Aarhus Universitets segl

Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. / Nilsson, Jakob; Sengupta, Jayati; Gursky, Richard; Kjeldgaard, Morten; Nissen, Poul; Frank, Joachim.

In: Journal of Molecular Biology, Vol. 382, No. 1, 2008, p. 179-187.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Nilsson, J, Sengupta, J, Gursky, R, Kjeldgaard, M, Nissen, P & Frank, J 2008, 'Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy', Journal of Molecular Biology, vol. 382, no. 1, pp. 179-187.

APA

Nilsson, J., Sengupta, J., Gursky, R., Kjeldgaard, M., Nissen, P., & Frank, J. (2008). Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. Journal of Molecular Biology, 382(1), 179-187.

CBE

Nilsson J, Sengupta J, Gursky R, Kjeldgaard M, Nissen P, Frank J. 2008. Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. Journal of Molecular Biology. 382(1):179-187.

MLA

Nilsson, Jakob et al. "Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy". Journal of Molecular Biology. 2008, 382(1). 179-187.

Vancouver

Nilsson J, Sengupta J, Gursky R, Kjeldgaard M, Nissen P, Frank J. Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. Journal of Molecular Biology. 2008;382(1):179-187.

Author

Nilsson, Jakob ; Sengupta, Jayati ; Gursky, Richard ; Kjeldgaard, Morten ; Nissen, Poul ; Frank, Joachim. / Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. In: Journal of Molecular Biology. 2008 ; Vol. 382, No. 1. pp. 179-187.

Bibtex

@article{13a50e30fba611dd8f9a000ea68e967b,
title = "Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy",
abstract = "In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis. This is the first visualization of a structure representing a transition-state complex on the ribosome. Tight interactions are observed between the factor's G domain and the large ribosomal subunit, as well as between domain IV and an intersubunit bridge. In contrast, some of the domains of eEF2 implicated in small subunit binding display a large degree of flexibility. Furthermore, we find support for a transition-state model conformation of the switch I region in this complex where the reoriented switch I region interacts with a conserved rRNA region of the 40S subunit formed by loops of the 18S RNA helices 8 and 14. This complex is structurally distinct from the eEF2-bound 80S ribosome complexes previously reported, and analysis of this map sheds light on the GTPase-coupled translocation mechanism.",
author = "Jakob Nilsson and Jayati Sengupta and Richard Gursky and Morten Kjeldgaard and Poul Nissen and Joachim Frank",
year = "2008",
language = "English",
volume = "382",
pages = "179--187",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy

AU - Nilsson, Jakob

AU - Sengupta, Jayati

AU - Gursky, Richard

AU - Kjeldgaard, Morten

AU - Nissen, Poul

AU - Frank, Joachim

PY - 2008

Y1 - 2008

N2 - In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis. This is the first visualization of a structure representing a transition-state complex on the ribosome. Tight interactions are observed between the factor's G domain and the large ribosomal subunit, as well as between domain IV and an intersubunit bridge. In contrast, some of the domains of eEF2 implicated in small subunit binding display a large degree of flexibility. Furthermore, we find support for a transition-state model conformation of the switch I region in this complex where the reoriented switch I region interacts with a conserved rRNA region of the 40S subunit formed by loops of the 18S RNA helices 8 and 14. This complex is structurally distinct from the eEF2-bound 80S ribosome complexes previously reported, and analysis of this map sheds light on the GTPase-coupled translocation mechanism.

AB - In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis. This is the first visualization of a structure representing a transition-state complex on the ribosome. Tight interactions are observed between the factor's G domain and the large ribosomal subunit, as well as between domain IV and an intersubunit bridge. In contrast, some of the domains of eEF2 implicated in small subunit binding display a large degree of flexibility. Furthermore, we find support for a transition-state model conformation of the switch I region in this complex where the reoriented switch I region interacts with a conserved rRNA region of the 40S subunit formed by loops of the 18S RNA helices 8 and 14. This complex is structurally distinct from the eEF2-bound 80S ribosome complexes previously reported, and analysis of this map sheds light on the GTPase-coupled translocation mechanism.

M3 - Journal article

VL - 382

SP - 179

EP - 187

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -