5mdr | pdb_00005mdr

Crystal structure of in vitro folded Chitoporin VhChip from Vibrio harveyi in complex with chitohexaose

spinqualitylabelsall models 5mdr, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mdr is a 6 chain structure with sequence from "achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C8E, NA, NAG NonStd Res: MSE Gene: chiP ("Achromobacter harveyi" Johnson and Shunk 1936) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Chitin, an insoluble polymer of N-acetylglucosamine, is one of the most abundant biopolymers on Earth. By degrading chitin, chitinolytic bacteria such as Vibrio harveyi are critical for chitin recycling and maintenance of carbon and nitrogen cycles in the world's oceans. A decisive step in chitin degradation is the uptake of chito-oligosaccharides by an outer membrane protein channel named chitoporin (ChiP). Here, we report X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides. Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel. Together with molecular dynamics simulations, electrophysiology and in vitro transport assays our data provide an explanation for the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport. Structural basis for chitin acquisition by marine Vibrio species.,Aunkham A, Zahn M, Kesireddy A, Pothula KR, Schulte A, Basle A, Kleinekathofer U, Suginta W, van den Berg B Nat Commun. 2018 Jan 15;9(1):220. doi: 10.1038/s41467-017-02523-y. PMID:29335469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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