2D1P

crystal structure of heterohexameric TusBCD proteins, which are crucial for the tRNA modification

Summary for 2D1P

• Entry DOI: 10.2210/pdb2d1p/pdb
• Descriptor: Hypothetical UPF0163 protein yheN, Hypothetical UPF0116 protein yheM, Hypothetical protein yheL, ... (5 entities in total)
• Functional Keywords: trna modification, sulfur transfer, structural genomics, translation
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Probable): P45532 P45531 P45530
• Total number of polymer chains: 9
• Total formula weight: 116621.99

Authors

Numata, T.,Fukai, S.,Ikeuchi, Y.,Suzuki, T.,Nureki, O. (deposition date: 2005-08-30, release date: 2006-02-28, Last modification date: 2024-03-13)

Primary citation

Numata, T.,Fukai, S.,Ikeuchi, Y.,Suzuki, T.,Nureki, O.
Structural Basis for Sulfur Relay to RNA Mediated by Heterohexameric TusBCD Complex
Structure, 14:357-366, 2006

PubMed Abstract: Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is exclusively modified into 2-thiouridine (s2U), which is crucial for both precise codon recognition and recognition by the cognate aminoacyl-tRNA synthetases. Recent Escherichia coli genetic studies revealed that the products of five novel genes, tusABCDE, function in the s2U modification. Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD complex, a sulfur transfer mediator, forming a heterohexamer composed of a dimer of the heterotrimer. Structure-based sequence alignment suggested two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in TusD), which are exposed on the hexameric complex. In vivo mutant analyses revealed that only Cys78, in the TusD subunit, participates in sulfur transfer during the s2U modification process. Since the single Cys acts as a catalytic residue, we proposed that TusBCD mediates sulfur relay via a putative persulfide state of the TusD subunit.

PubMed: 16472754
DOI: 10.1016/j.str.2005.11.009

Experimental method

X-RAY DIFFRACTION (2.15 Å)