Structural model for the selenocysteine-specific elongation factor SelB

R. Hilgenfeld; A. Böck; R. Wilting

doi:10.1016/S0300-9084(97)86719-3

Structural model for the selenocysteine-specific elongation factor SelB

R. Hilgenfeld, A. Böck, R. Wilting^*

^*Corresponding author for this work

Institute of Biochemistry

27 Citations (Scopus)

Abstract

A structural model was established for the N-terminal part of translation factor SelB which shares sequence similarity with EF-Tu, taking into account the coordinates of the EF-Tu 3D structure and the consensus of SelB sequences from four bacteria. The model showed that SelB is homologous in its N-terminal domains over all three domains of EF-Tu. The guanine nucleotide binding site and the residues involved in GTP hydrolysis are similar to those of EF-Tu, but with some subtle differences possibly responsible for the higher affinity of SelB for GTP compared to GDP. In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB. Information on the formation of the selenocysteyl-binding pocket is presented. A phylogenetic comparison of the SelB domains homologous to EF-Tu with those from EF-Tu and initiation factor 2 indicated that SelB forms a separate class of translation factors.

Original language	English
Journal	Biochimie
Volume	78
Issue number	11-12
Pages (from-to)	971-978
Number of pages	8
ISSN	0300-9084
DOIs	https://doi.org/10.1016/S0300-9084(97)86719-3
Publication status	Published - 1996

Funding

We thank H Schtitz for help with computer calculations. This work was supported by grants from the Deutsche Forschungsgemein- schaft (SFB 369), from the DESY-PS, 7rom European Commission via its Human Capital and Mobility Programme, and from the Fonds der Chemischen lndustrie.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/S0300-9084(97)86719-3

Cite this

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title = "Structural model for the selenocysteine-specific elongation factor SelB",

abstract = "A structural model was established for the N-terminal part of translation factor SelB which shares sequence similarity with EF-Tu, taking into account the coordinates of the EF-Tu 3D structure and the consensus of SelB sequences from four bacteria. The model showed that SelB is homologous in its N-terminal domains over all three domains of EF-Tu. The guanine nucleotide binding site and the residues involved in GTP hydrolysis are similar to those of EF-Tu, but with some subtle differences possibly responsible for the higher affinity of SelB for GTP compared to GDP. In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB. Information on the formation of the selenocysteyl-binding pocket is presented. A phylogenetic comparison of the SelB domains homologous to EF-Tu with those from EF-Tu and initiation factor 2 indicated that SelB forms a separate class of translation factors.",

author = "R. Hilgenfeld and A. B{\"o}ck and R. Wilting",

note = "Funding Information: We thank H Schtitz for help with computer calculations. This work was supported by grants from the Deutsche Forschungsgemein- Funding Information: schaft (SFB 369), from the DESY-PS, 7rom European Commission via its Human Capital and Mobility Programme, and from the Fonds der Chemischen lndustrie. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

year = "1996",

doi = "10.1016/S0300-9084(97)86719-3",

language = "English",

volume = "78",

pages = "971--978",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier B.V.",

number = "11-12",

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TY - JOUR

T1 - Structural model for the selenocysteine-specific elongation factor SelB

AU - Hilgenfeld, R.

AU - Böck, A.

AU - Wilting, R.

N1 - Funding Information: We thank H Schtitz for help with computer calculations. This work was supported by grants from the Deutsche Forschungsgemein- Funding Information: schaft (SFB 369), from the DESY-PS, 7rom European Commission via its Human Capital and Mobility Programme, and from the Fonds der Chemischen lndustrie. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 1996

Y1 - 1996

N2 - A structural model was established for the N-terminal part of translation factor SelB which shares sequence similarity with EF-Tu, taking into account the coordinates of the EF-Tu 3D structure and the consensus of SelB sequences from four bacteria. The model showed that SelB is homologous in its N-terminal domains over all three domains of EF-Tu. The guanine nucleotide binding site and the residues involved in GTP hydrolysis are similar to those of EF-Tu, but with some subtle differences possibly responsible for the higher affinity of SelB for GTP compared to GDP. In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB. Information on the formation of the selenocysteyl-binding pocket is presented. A phylogenetic comparison of the SelB domains homologous to EF-Tu with those from EF-Tu and initiation factor 2 indicated that SelB forms a separate class of translation factors.

AB - A structural model was established for the N-terminal part of translation factor SelB which shares sequence similarity with EF-Tu, taking into account the coordinates of the EF-Tu 3D structure and the consensus of SelB sequences from four bacteria. The model showed that SelB is homologous in its N-terminal domains over all three domains of EF-Tu. The guanine nucleotide binding site and the residues involved in GTP hydrolysis are similar to those of EF-Tu, but with some subtle differences possibly responsible for the higher affinity of SelB for GTP compared to GDP. In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB. Information on the formation of the selenocysteyl-binding pocket is presented. A phylogenetic comparison of the SelB domains homologous to EF-Tu with those from EF-Tu and initiation factor 2 indicated that SelB forms a separate class of translation factors.

UR - https://www.scopus.com/pages/publications/0030425121

U2 - 10.1016/S0300-9084(97)86719-3

DO - 10.1016/S0300-9084(97)86719-3

M3 - Journal articles

C2 - 9150874

AN - SCOPUS:0030425121

SN - 0300-9084

VL - 78

SP - 971

EP - 978

JO - Biochimie

JF - Biochimie

IS - 11-12

ER -

Structural model for the selenocysteine-specific elongation factor SelB

Abstract

Funding

UN SDGs

Research Areas and Centers

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