1Z43
Crystal structure of 7S.S SRP RNA of M. jannaschii
Summary for 1Z43
| Entry DOI | 10.2210/pdb1z43/pdb |
| Related | 1LNG |
| Descriptor | RNA (101-MER) (2 entities in total) |
| Functional Keywords | rna, tetra-loop |
| Total number of polymer chains | 1 |
| Total formula weight | 32769.54 |
| Authors | Hainzl, T.,Huang, S.,Sauer-Eriksson, A.E. (deposition date: 2005-03-15, release date: 2005-06-14, Last modification date: 2023-10-25) |
| Primary citation | Hainzl, T.,Huang, S.,Sauer-Eriksson, A.E. Structural insights into SRP RNA: An induced fit mechanism for SRP assembly Rna, 11:1043-1050, 2005 Cited by PubMed Abstract: Proper assembly of large protein-RNA complexes requires sequential binding of the proteins to the RNA. The signal recognition particle (SRP) is a multiprotein-RNA complex responsible for the cotranslational targeting of proteins to biological membranes. Here we describe the crystal structure at 2.6-A resolution of the S-domain of SRP RNA from the archeon Methanococcus jannaschii. Comparison of this structure with the SRP19-bound form reveals the nature of the SRP19-induced conformational changes, which promote subsequent SRP54 attachment. These structural changes are initiated at the SRP19 binding site and transmitted through helix 6 to looped-out adenosines, which form tertiary RNA interaction with helix 8. Displacement of these adenosines enforces a conformational change of the asymmetric loop structure in helix 8. In free RNA, the three unpaired bases A195, C196, and C197 are directed toward the helical axis, whereas upon SRP19 binding the loop backbone inverts and the bases are splayed out in a conformation that resembles the SRP54-bound form. Nucleotides adjacent to the bulged nucleotides seem to be particularly important in the regulation of this loop transition. Binding of SRP19 to 7S RNA reveals an elegant mechanism of how protein-induced changes are directed through an RNA molecule and may relate to those regulating the assembly of other RNPs. PubMed: 15928341DOI: 10.1261/rna.2080205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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