4lbv

Identifying ligand binding hot spots in proteins using brominated fragments

spinqualitylabelsall models 4lbv, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lbv is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Ligands: CL, GNP, MG, NH4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EFTU1_THETH This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Publication Abstract from PubMed High-quality crystals of Thermus thermophilus EF-Tu in the GTP-bound conformation at 1.7-2.7 A resolution were used to test 18 small organic molecules, all brominated for confident identification in the anomalous difference maps. From this relatively small collection, it was possible to identify a small molecule bound in the functionally important tRNA CCA-end binding pocket. The antibiotic GE2270 A is known to interact with the same pocket in EF-Tu and to disrupt the association with tRNA. Bromide could be located from peaks in the anomalous map in data truncated to very low resolution without refining the structure. Considering the speed with which diffraction data can be collected today, it is proposed that it is worthwhile to collect the extra data from fragment screens while crystals are at hand to increase the knowledge of biological function and drug binding in an experimental structural context. Identifying ligand-binding hot spots in proteins using brominated fragments.,Groftehauge MK, Therkelsen MO, Taaning R, Skrydstrup T, Morth JP, Nissen P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):1060-5. doi: , 10.1107/S1744309113018551. Epub 2013 Aug 19. PMID:23989163 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures

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