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1JID

Human SRP19 in complex with helix 6 of Human SRP RNA

Summary for 1JID
Entry DOI10.2210/pdb1jid/pdb
Related1D4R
DescriptorHELIX 6 OF HUMAN SRP RNA, SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordssignal recognition particle (srp), protein-rna complex, ggag tetraloop, signaling protein-rna complex, signaling protein/rna
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: P09132
Total number of polymer chains2
Total formula weight24468.11
Authors
Wild, K.,Sinning, I.,Cusack, S. (deposition date: 2001-07-02, release date: 2001-10-19, Last modification date: 2023-08-16)
Primary citationWild, K.,Sinning, I.,Cusack, S.
Crystal structure of an early protein-RNA assembly complex of the signal recognition particle.
Science, 294:598-601, 2001
Cited by
PubMed Abstract: The signal recognition particle (SRP) is a universally conserved ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to cellular membranes. A crucial early step in SRP assembly in archaea and eukarya is the binding of protein SRP19 to specific sites on SRP RNA. Here we report the 1.8 angstrom resolution crystal structure of human SRP19 in complex with its primary binding site on helix 6 of SRP RNA, which consists of a stem-loop structure closed by an unusual GGAG tetraloop. Protein-RNA interactions are mediated by the specific recognition of a widened major groove and the tetraloop without any direct protein-base contacts and include a complex network of highly ordered water molecules. A model of the assembly of the SRP core comprising SRP19, SRP54, and SRP RNA based on crystallographic and biochemical data is proposed.
PubMed: 11641499
DOI: 10.1126/science.1063839
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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