3PUZ

Crystal Structure of a pre-translocation state MBP-Maltose transporter complex bound to AMP-PNP

Summary for 3PUZ

• Entry DOI: 10.2210/pdb3puz/pdb
• Related: 3puv 3puw 3pux 3puy 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: 216978.10

Authors

Oldham, M.L.,Chen, J. (deposition date: 2010-12-06, release date: 2011-05-18, Last modification date: 2024-10-16)

Primary citation

Oldham, M.L.,Chen, J.
Crystal structure of the maltose transporter in a pretranslocation intermediate state.
Science, 332:1202-1205, 2011

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: 21566157
DOI: 10.1126/science.1200767

Experimental method

X-RAY DIFFRACTION (2.9 Å)