5l3s | pdb_00005l3s

Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY

spinqualitylabelsall models 5l3s, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l3s is a 8 chain structure with sequence from Sacs2 and Sulac. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GNP, GOL, MG, SO4 Gene: srp54, SSO0971 (SACS2), ftsY, dpa, sso, Saci_1462 (SULAC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SRP54_SULSO] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity). [FTSY_SULAC] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).[HAMAP-Rule:MF_00920] Publication Abstract from PubMed The signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life. Here, we present the crystal structures of the GTPase heterodimers of archaeal (Sulfolobus solfataricus), eukaryotic (Homo sapiens), and chloroplast (Arabidopsis thaliana) SRP systems. The comprehensive structural comparison combined with Brownian dynamics simulations of TC formation allows for the description of the general blueprint and of specific adaptations of the quasi-symmetric heterodimer. Our work defines conserved external nucleotide-binding sites for SRP GTPase activation by RNA. Structural analyses of the GDP-bound, post-hydrolysis states reveal a conserved, magnesium-sensitive switch within the I-box. Overall, we provide a general model for SRP cycle regulation by RNA. Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex.,Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309 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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