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1LN4

CRYSTAL STRUCTURE OF E. COLI YHBY

Summary for 1LN4
Entry DOI10.2210/pdb1ln4/pdb
DescriptorHypothetical protein yhbY (2 entities in total)
Functional Keywordsputative rna-binding protein; putative translation factor, rna binding protein
Biological sourceEscherichia coli
Cellular locationCytoplasm: P42550
Total number of polymer chains1
Total formula weight11717.67
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 citationOstheimer, 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: 12429100
DOI: 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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數據於2025-07-23公開中

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