3PUY
Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to AMP-PNP after crystal soaking of the pretranslocation state
Summary for 3PUY
| Entry DOI | 10.2210/pdb3puy/pdb |
| Related | 3puv 3puw 3pux 3puz 3pv0 |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltose transporter subunit; periplasmic-binding component of ABC superfamily, Maltose transporter subunit; membrane component of ABC superfamily, Fused maltose transport subunit, ATP-binding component of ABC superfamily; regulatory protein, ... (9 entities in total) |
| Functional Keywords | atp binding cassette, nucleotide binding domain, substrate binding protein, abc transporter, importer, atpase, atp binding, maltodextrin binding, transmembrane integral membrane, transport protein, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 5 |
| Total formula weight | 217442.55 |
| Authors | Oldham, M.L.,Chen, J. (deposition date: 2010-12-06, release date: 2011-05-18, Last modification date: 2023-09-06) |
| Primary citation | Oldham, M.L.,Chen, J. Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science, 332:1202-1205, 2011 Cited by PubMed Abstract: Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert chemical energy from ATP hydrolysis to mechanical work for substrate translocation. They function by alternating between two states, exposing the substrate-binding site to either side of the membrane. A key question that remains to be addressed is how substrates initiate the transport cycle. Using x-ray crystallography, we have captured the maltose transporter in an intermediate step between the inward- and outward-facing states. We show that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state. These results, interpreted in light of biochemical and functional studies, provide a structural basis to understand allosteric communication in ABC transporters. PubMed: 21566157DOI: 10.1126/science.1200767 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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