3RLF

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

Summary for 3RLF

• Entry DOI: 10.2210/pdb3rlf/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, Maltose transport system permease protein malF, Maltose transport system permease protein malG, ... (10 entities in total)
• Functional Keywords: integral membrane protein, atpase, abc transporter, membrane, transmembrane, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 220462.45

Authors

Oldham, M.L.,Chen, J. (deposition date: 2011-04-19, release date: 2011-08-10, Last modification date: 2023-09-13)

Primary citation

Oldham, M.L.,Chen, J.
Snapshots of the maltose transporter during ATP hydrolysis.
Proc.Natl.Acad.Sci.USA, 108:15152-15156, 2011

PubMed Abstract: 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'-(β,γ-imido)triphosphate or ADP in conjunction with phosphate analogs BeF(3)(-), VO(4)(3-), or AIF(4)(-), were determined to 2.2- to 2.4-Å 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.

PubMed: 21825153
DOI: 10.1073/pnas.1108858108

Experimental method

X-RAY DIFFRACTION (2.2 Å)