3RLF: Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp

Citation:
Proc. Natl. Acad. Sci. U. S. A. (2011) 108 p.15152-15156
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'-(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.
PDB ID: 3RLFDownload
MMDB ID: 92560
PDB Deposition Date: 2011/4/19
Updated in MMDB: 2011/09
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 3RLF: pentameric; determined by author and by software (PISA)
Molecular Components in 3RLF
Label Count Molecule
Proteins (5 molecules)
1
Maltose-binding Periplasmic Protein(Gene symbol: malE)
Molecule annotation
1
Maltose Transport System Permease Protein Malf(Gene symbol: malF)
Molecule annotation
1
Maltose Transport System Permease Protein Malg(Gene symbol: malG)
Molecule annotation
2
Maltose/maltodextrin Import Atp-binding Protein Malk(Gene symbol: malK)
Molecule annotation
Chemicals (10 molecules)
1
1
2
1
3
4
4
2
5
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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