2j7p

GMPPNP-STABILIZED NG DOMAIN COMPLEX OF THE SRP GTPASES FFH AND FTSY

spinqualitylabelsall models 2j7p, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j7p is a 4 chain structure with sequence from Atcc 25104. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, GNP, IOD, K, MG Related: 1ffh, 1jpj, 1jpn, 1ls1, 1ng1, 1o87, 1okk, 1rj9, 1ry1, 2c03, 2c04, 2cnw, 2ffh, 2j45, 2j46, 2ng1, 3ng1, 2iyl Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [FTSY_THEAQ] 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) (By similarity). 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 Ffh and FtsY are GTPase components of the signal recognition particle co-translational targeting complex that assemble during the SRP cycle to form a GTP-dependent and pseudo twofold symmetric heterodimer. Previously the SRP GTPase heterodimer has been stabilized and purified for crystallographic studies using both the non-hydrolysable GTP analog GMPPCP and the pseudo-transition state analog GDP:AlF4, revealing in both cases a buried nucleotide pair that bridges and forms a key element of the heterodimer interface. A complex of Ffh and FtsY from Thermus aquaticus formed in the presence of the analog GMPPNP could not be obtained, however. The origin of this failure was previously unclear, and it was thought to have arisen from either instability of the analog, or, alternatively, from differences in its interactions within the tightly conscribed composite active site chamber of the complex. Using insights gained from the previous structure determinations, we have now determined the structure of the SRP GTPase targeting heterodimer stabilized by the non-hydrolysable GTP analog GMPPNP. The structure demonstrates how the different GTP analogs are accommodated within the active site chamber despite slight differences in the geometry of the phosphate chain. It also reveals a K+ coordination site at the highly conserved DARGG loop at the N/G interdomain interface. Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.,Gawronski-Salerno J, Freymann DM J Struct Biol. 2007 Apr;158(1):122-8. Epub 2006 Nov 3. PMID:17184999 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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