Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu

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Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. / Thirup, Søren Skou; Van, Lan Bich; Nielsen, Tine K; Knudsen, Charlotte R.

In: Journal of Structural Biology, Vol. 191, No. 1, 11.06.2015, p. 10-21.

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@article{5c2e15ee57704a6e9ba45362832e019d,
title = "Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu",
abstract = "Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8 {\AA} resolution), EF-Tu:PO4:EF-Ts (1.9 {\AA} resolution), EF-Tu:GDPNP:EF-Ts (2.2 {\AA} resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5 {\AA} resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.",
author = "Thirup, {S{\o}ren Skou} and Van, {Lan Bich} and Nielsen, {Tine K} and Knudsen, {Charlotte R}",
note = "Copyright {\circledC} 2015. Published by Elsevier Inc.",
year = "2015",
month = "6",
day = "11",
doi = "10.1016/j.jsb.2015.06.011",
language = "English",
volume = "191",
pages = "10--21",
journal = "Journal of Structural Biology",
issn = "1047-8477",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu

AU - Thirup, Søren Skou

AU - Van, Lan Bich

AU - Nielsen, Tine K

AU - Knudsen, Charlotte R

N1 - Copyright © 2015. Published by Elsevier Inc.

PY - 2015/6/11

Y1 - 2015/6/11

N2 - Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8 Å resolution), EF-Tu:PO4:EF-Ts (1.9 Å resolution), EF-Tu:GDPNP:EF-Ts (2.2 Å resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5 Å resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.

AB - Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8 Å resolution), EF-Tu:PO4:EF-Ts (1.9 Å resolution), EF-Tu:GDPNP:EF-Ts (2.2 Å resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5 Å resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.

U2 - 10.1016/j.jsb.2015.06.011

DO - 10.1016/j.jsb.2015.06.011

M3 - Journal article

C2 - 26073967

VL - 191

SP - 10

EP - 21

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

IS - 1

ER -