3ppr

Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC

spinqualitylabelsall models 3ppr, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ppr is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 4CS Related: 3ppn, 3ppo, 3ppp, 3ppq Gene: opuCC ("Bacillus globigii" Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [OPUCC_BACSU] Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline. Publication Abstract from PubMed The compatible solute ATP-binding cassette (ABC) transporters are indispensable for acquiring a variety of compatible solutes under osmotic stress in Bacillus subtilis. The substrate-binding protein OpuCC of the ABC transporter OpuC can recognize a broad spectrum of compatible solutes, compared to its 70% sequence-identical paralog OpuBC that can solely bind choline. To explore the structural basis of this difference of substrate specificity, we determined crystal structures of OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with substrate-binding pocket located at the inter-domain cleft. Upon substrate-binding, the two domains shift towards each other to trap the substrate. Comparative structural analysis revealed a plastic pocket that fits various compatible solutes, which attributes the multiple-substrate binding property to OpuCC. This plasticity is a gain-of-function via a single-residue mutation of Thr94 in OpuCC versus Asp96 in OpuBC. Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC.,Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y Biochem J. 2011 Mar 3. PMID:21366542 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter

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