2xxa | pdb_00002xxa

THE CRYSTAL STRUCTURE OF THE SIGNAL RECOGNITION PARTICLE (SRP) IN COMPLEX WITH ITS RECEPTOR(SR)

spinqualitylabelsall models 2xxa, resolution 3.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xxa is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GCP, MG Related: 1dul, 2xkv, 2j28, 1hq1, 1fts Activity: Signal-recognition-particle GTPase, with EC number 3.6.5.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon. The crystal structure of the signal recognition particle in complex with its receptor.,Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N Science. 2011 Feb 18;331(6019):881-6. PMID:21330537 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Signal recognition particle protein Signal recognition particle receptor

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