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 - http://www.scopus.com/inward/record.url?scp=0030425121&partnerID=8YFLogxK
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 -
