3pux | pdb_00003pux

Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-BeF3

spinqualitylabelsall models 3pux, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pux is a 5 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 2.3Å Ligands: ADP, BEF, GLC, MG, PGV, PRD_900001, UMQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALG_ECOLI Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. Publication Abstract from PubMed ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(beta,gamma-imido)triphosphate or ADP in conjunction with phosphate analogs , , or , were determined to 2.2- to 2.4-A resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism. Snapshots of the maltose transporter during ATP hydrolysis.,Oldham ML, Chen J Proc Natl Acad Sci U S A. 2011 Aug 8. PMID:21825153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Maltose-binding protein 3D structures

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