4G4P
Crystal structure of glutamine-binding protein from Enterococcus faecalis at 1.5 A
Summary for 4G4P
| Entry DOI | 10.2210/pdb4g4p/pdb |
| Descriptor | Amino acid ABC transporter, amino acid-binding/permease protein, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTAMINE, ... (4 entities in total) |
| Functional Keywords | substrate-binding domain, abc transporter, glutamine/glutamate binding, transport protein |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 1 |
| Total formula weight | 27638.94 |
| Authors | Fulyani, F.,Guskov, A.,Zagar, A.V.,Slotboom, D.-J.,Poolman, B. (deposition date: 2012-07-16, release date: 2013-07-17, Last modification date: 2024-02-28) |
| Primary citation | Fulyani, F.,Schuurman-Wolters, G.K.,Zagar, A.V.,Guskov, A.,Slotboom, D.J.,Poolman, B. Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria. Structure, 21:1879-1888, 2013 Cited by PubMed Abstract: 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. PubMed: 23994008DOI: 10.1016/j.str.2013.07.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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