2wit

CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE

spinqualitylabelsall models 2wit, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wit is a 3 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. This structure supersedes the now removed PDB entry 2w8a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BET NonStd Res: MSE Related: 2w8a Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BETP_CORGL] High-affinity uptake of glycine betaine (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 Osmoregulated transporters sense intracellular osmotic pressure and respond to hyperosmotic stress by accumulation of osmolytes to restore normal hydration levels. Here we report the determination of the X-ray structure of a member of the family of betaine/choline/carnitine transporters, the Na(+)-coupled symporter BetP from Corynebacterium glutamicum, which is a highly effective osmoregulated uptake system for glycine betaine. Glycine betaine is bound in a tryptophan box occluded from both sides of the membrane with aromatic side chains lining the transport pathway. BetP has the same overall fold as three unrelated Na(+)-coupled symporters. Whereas these are crystallized in either the outward-facing or the inward-facing conformation, the BetP structure reveals a unique intermediate conformation in the Na(+)-coupled transport cycle. The trimeric architecture of BetP and the break in three-fold symmetry by the osmosensing C-terminal helices suggest a regulatory mechanism of Na(+)-coupled osmolyte transport to counteract osmotic stress. Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP.,Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C Nature. 2009 Mar 5;458(7234):47-52. PMID:19262666 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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