6ghu

Crystal structure of the periplasmic domain of XcpY, oP crystal form.Crystal structure of the periplasmic domain of XcpY, oP crystal form.

Structural highlights 6ghu is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. This structure supersedes the now removed PDB entry 5n7s. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5n7l Gene: xcpY, PAMH19_1972 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A0A8RGG2_PSEAI] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins.[PIRNR:PIRNR015761] Publication Abstract from PubMed The ability of bacteria to infect a host relies in part on the secretion of molecular virulence factors across the cell envelope. Pseudomonas aeruginosa, a ubiquitous environmental bacterium causing opportunistic infections in humans, employs the type II secretion system (T2SS) to transport effector proteins across its cellular envelope as part of a diverse array of virulence strategies. General secretory pathway protein L (GspL) is an essential inner-membrane component of the T2SS apparatus, and is thought to facilitate transduction of the energy from ATP hydrolysis in the cytoplasm to the periplasmic components of the system. However, our incomplete understanding of the assembly principles of the T2SS machinery prevents the mechanistic deconvolution of T2SS-mediated protein secretion. Here we show via two crystal structures that the periplasmic ferredoxin-like domain of GspL (GspL(fld)) is a dimer stabilized by hydrophobic interactions, and that this interface may allow significant interdomain plasticity. The general dimerization mode of GspL(fld) is shared with GspL from Vibrio parahaemolyticus suggesting a conserved oligomerization mode across the GspL family. Furthermore, we identified a tetrameric form of the complete periplasmic segment of GspL (GspL(peri)) which indicates that GspL may be able to adopt multiple oligomeric states as part of its dynamic role in the T2SS apparatus. Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.,Fulara A, Vandenberghe I, Read RJ, Devreese B, Savvides SN Sci Rep. 2018 Nov 13;8(1):16760. doi: 10.1038/s41598-018-34956-w. PMID:30425318 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6ghu, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image