InterPro : IPR009000

Name  Translation protein, beta-barrel domain Short Name  Transl_B-barrel
Type  Domain Description  A beta barrel of circularly permuted topology is found in many transcription proteins, including initiation and elongation factors, and also some ribosomal proteins, although in these cases the fold is elaborated with additional structures. The beta barrel domain is represented by domain 2 of the elongation factors EF-Tu []and eEF1A [], both of which function to recognise and transport aminoacyl-tRNA to the acceptor (A) site of the ribosome during the elongation process, and of EF-G [], which functions in translocating the peptidyl tRNA from the A site to the peptidyl (P) site. This domain is also present in initiation factors, in domain 2 of eIF2 gamma subunit [], and domains 2 and 4 of IF2/eIF5B [], both of which function to transport the initiator methionyl-tRNA to the ribosome. This beta barrel domain may be involved in interactions with the switch 2 region to stabilise the relative orientations of the domains, which undergo functionally important conformational changes between GTP- and GDP-bound states.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR004161 Translation elongation factor EFTu/EF1A, domain 2 Transl_elong_EFTu/EF1A_2 Domain
IPR029459 Elongation factor Tu-type domain EFTU-type Domain

1 Contains

Id Name Short Name Type
IPR019926 Ribosomal protein L3, conserved site Ribosomal_L3_CS Conserved_site

6 Found In

Id Name Short Name Type
IPR004540 Translation elongation factor EFG/EF2 Transl_elong_EFG/EF2 Family
IPR004541 Translation elongation factor EFTu/EF1A, bacterial/organelle Transl_elong_EFTu/EF1A_bac/org Family
IPR022424 Translation initiation factor 2, gamma subunit TIF2_gsu Family
IPR004543 Translation elongation factor EFG/EF2, archaeal Transl_elong_EFG/EF2_arc Family
IPR006297 Elongation factor 4 EF-4 Family
IPR016744 Uncharacterised conserved protein UCP019072 UCP019072 Family

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Laurberg M Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. 2000 J Mol Biol 303 593-603
Andersen GR Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. 2000 Mol Cell 6 1261-6
Andersen GR High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. 2000 J Mol Biol 297 421-36
Schmitt E The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. 2002 EMBO J 21 1821-32
Roll-Mecak A X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. 2000 Cell 103 781-92



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)