4g4p

Crystal structure of glutamine-binding protein from Enterococcus faecalis at 1.5 A

spinqualitylabelsall models 4g4p, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g4p is a 1 chain structure with sequence from Enterococcus faecalis V583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLN, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q837S0_ENTFA Publication Abstract from PubMed The ATP-binding cassette (ABC) transporter GlnPQ is an essential uptake system for amino acids in gram-positive pathogens and related nonpathogenic bacteria. The transporter has tandem substrate-binding domains (SBDs) fused to each transmembrane domain, giving rise to four SBDs per functional transporter complex. We have determined the crystal structures and ligand-binding properties of the SBDs of GlnPQ from Enterococcus faecalis, Streptococcus pneumoniae, and Lactococcus lactis. The tandem SBDs differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. The combined structural, functional, and thermodynamic analysis revealed the roles of individual residues in determining the substrate affinity. We succeeded in converting a low-affinity SBD into a high-affinity receptor and vice versa. Our data indicate that a small number of residues that reside in the binding pocket constitute the major affinity determinants of the SBDs. Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria.,Fulyani F, Schuurman-Wolters GK, Zagar AV, Guskov A, Slotboom DJ, Poolman B Structure. 2013 Aug 28. pii: S0969-2126(13)00270-0. doi:, 10.1016/j.str.2013.07.020. PMID:23994008 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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