2UWM

C-TERMINAL DOMAIN(WH2-WH4) OF ELONGATION FACTOR SELB IN COMPLEX WITH SECIS RNA

Summary for 2UWM

• Entry DOI: 10.2210/pdb2uwm/pdb
• Descriptor: SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR, 5'-R(*GP*GP*CP*GP*UP*UP*GP*CP*CP*GP *GP*UP*CP*UP*GP*GP*CP*AP*AP*CP*GP*CP*C)-3' (3 entities in total)
• Functional Keywords: protein biosynthesis, translation, gtp-binding, nucleotide- binding, selenocysteine-specific elongation factor
• Biological source: MOORELLA THERMOACETICA; More
• Total number of polymer chains: 4
• Total formula weight: 74154.17

Authors

Ose, T.,Soler, N.,Rasubala, L.,Kuroki, K.,Kohda, D.,Fourmy, D.,Yoshizawa, S.,Maenaka, K. (deposition date: 2007-03-22, release date: 2007-05-08, Last modification date: 2023-12-13)

Primary citation

Ose, T.,Soler, N.,Rasubala, L.,Kuroki, K.,Kohda, D.,Fourmy, D.,Yoshizawa, S.,Maenaka, K.
Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor Selb.
Structure, 15:577-, 2007

PubMed Abstract: Selenocysteine (Sec) is the "21st" amino acid and is genetically encoded by an unusual incorporation system. The stop codon UGA becomes a Sec codon when the selenocysteine insertion sequence (SECIS) exists downstream of UGA. Sec incorporation requires a specific elongation factor, SelB, which recognizes tRNA(Sec) via use of an EF-Tu-like domain and the SECIS mRNA hairpin via use of a C-terminal domain (SelB-C). SelB functions in multiple translational steps: binding to SECIS mRNA and tRNA(Sec), delivery of tRNA(Sec) onto an A site, GTP hydrolysis, and release from tRNA and mRNA. However, this dynamic mechanism remains to be revealed. Here, we report a large domain rearrangement in the structure of SelB-C complexed with RNA. Surprisingly, the interdomain region forms new interactions with the phosphate backbone of a neighboring RNA, distinct from SECIS RNA binding. This SelB-RNA interaction is sequence independent, possibly reflecting SelB-tRNA/-rRNA recognitions. Based on these data, the dynamic SelB-ribosome-mRNA-tRNA interactions will be discussed.

PubMed: 17502103
DOI: 10.1016/J.STR.2007.03.007

Experimental method

X-RAY DIFFRACTION (2.31 Å)