2y5y | pdb_00002y5y

Crystal structure of LacY in complex with an affinity inactivator

spinqualitylabelsall models 2y5y, resolution 3.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y5y is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.38Å Ligands: BA, TGA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LACY_ECOLI Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Publication Abstract from PubMed Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies. Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition.,Chaptal V, Kwon S, Sawaya MR, Guan L, Kaback HR, Abramson J Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9361-6. Epub 2011 May 18. PMID:21593407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactose Permease

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