3rlf | pdb_00003rlf

Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to MgAMPPNP

spinqualitylabelsall models 3rlf, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rlf is a 5 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, GLC, MG, PGV, UMQ Gene: malE, b4034, JW3994 (ECOLI), malF, b4033, JW3993 (ECOLI), malG, b4032, JW3992 (ECOLI), malK, b4035, JW3995 (ECOLI) Activity: Maltose-transporting ATPase, with EC number 3.6.3.19 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MALK_ECOLI] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. [MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. [MALG_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [MALF_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 Ubiquitin protein ligase 3D structures

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