2j37

MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS

spinqualitylabelsall models 2j37, resolution 8.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j37 is a 8 chain structure with sequence from Canis sp., Haloarcula marismortui, Homo sapiens and Triticum sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1dul, 1hq1, 1p85, 1p86, 2aw4, 2awb, 2j28 Resources: FirstGlance, OCA, RCSB, PDBsum Function [SRP54_CANFA] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). [SRP19_HUMAN] Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting. Following the signal sequence from ribosomal tunnel exit to signal recognition particle.,Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R Nature. 2006 Nov 23;444(7118):507-11. Epub 2006 Oct 29. PMID:17086193 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L23 Ribosomal protein L31 Ribosomal protein L35 Signal recognition particle protein

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