1LN4
CRYSTAL STRUCTURE OF E. COLI YHBY
Summary for 1LN4
Entry DOI | 10.2210/pdb1ln4/pdb |
Descriptor | Hypothetical protein yhbY (2 entities in total) |
Functional Keywords | putative rna-binding protein; putative translation factor, rna binding protein |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P42550 |
Total number of polymer chains | 1 |
Total formula weight | 11717.67 |
Authors | Ostheimer, G.J.,Barkan, A.,Matthews, B.W. (deposition date: 2002-05-02, release date: 2002-05-15, Last modification date: 2024-02-14) |
Primary citation | Ostheimer, G.J.,Barkan, A.,Matthews, B.W. Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins Structure, 10:1593-1601, 2002 Cited by PubMed Abstract: E. coli YhbY belongs to a conserved family of hypothetical proteins represented in eubacteria, archaea, and plants (Pfam code UPF0044). Three maize proteins harboring UPF0044-like domains are required for chloroplast group II intron splicing, and bioinformatic data suggest a role for prokaryotic UPF0044 members in translation. The crystal structure of YhbY has been determined. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome. Modeling studies indicate that the same surface is highly basic in all members of UPF0044, suggesting a conserved RNA binding surface. Taken together, the evidence suggests that members of UPF0044 constitute a previously unrecognized class of RNA binding domain. PubMed: 12429100DOI: 10.1016/S0969-2126(02)00886-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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