3qf4 | pdb_00003qf4

Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation

spinqualitylabelsall models 3qf4, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qf4 is a 2 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, MG Related: 3qf5 Gene: TM_0287 (ATCC 43589), TM_0288 (ATCC 43589) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell membranes by alternating between inward- and outward-facing conformations, harnessing the energy of ATP binding and hydrolysis at their nucleotide binding domains (NBDs). Here we present the 2.9-A crystal structure of the heterodimeric ABC transporter TM287-TM288 (TM287/288) from Thermotoga maritima in its inward-facing state. In contrast to previous studies, we found that the NBDs only partially separate, remaining in contact through an interface involving conserved motifs that connect the two ATP hydrolysis sites. We observed AMP-PNP binding to the degenerate catalytic site, which deviates from the consensus sequence in the same positions as the eukaryotic homologs CFTR and TAP1-TAP2 (TAP1/2). The TM287/288 structure provides unprecedented insights into the mechanism of heterodimeric ABC exporters and will enable future studies on this large transporter superfamily. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation.,Hohl M, Briand C, Grutter MG, Seeger MA Nat Struct Mol Biol. 2012 Mar 25;19(4):395-402. doi: 10.1038/nsmb.2267. PMID:22447242 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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