» Articles » PMID: 21825153

Snapshots of the Maltose Transporter During ATP Hydrolysis

Overview
Specialty Science
Date 2011 Aug 10
PMID 21825153
Citations 101
Authors
Affiliations
Soon will be listed here.
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.

Citing Articles

Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16.

An N, Huang X, Yang Z, Zhang M, Ma M, Yu F Nat Plants. 2024; 10(12):2052-2061.

PMID: 39496849 DOI: 10.1038/s41477-024-01839-0.


Functional Roles of the Conserved Amino Acid Sequence Motif C, the Antiporter Motif, in Membrane Transporters of the Major Facilitator Superfamily.

Varela M, Ortiz-Alegria A, Lekshmi M, Stephen J, Kumar S Biology (Basel). 2023; 12(10).

PMID: 37887046 PMC: 10604125. DOI: 10.3390/biology12101336.


W546 stacking disruption traps the human porphyrin transporter ABCB6 in an outward-facing transient state.

Lee S, Park J, Jang E, Choi S, Kim S, Kim J Commun Biol. 2023; 6(1):960.

PMID: 37735522 PMC: 10514269. DOI: 10.1038/s42003-023-05339-3.


Binding Specificity of a Novel Cyclo/Maltodextrin-Binding Protein and Its Role in the Cyclodextrin ABC Importer System from Thermoanaerobacterales.

Aranda-Caraballo J, Saenz R, Lopez-Zavala A, Velazquez-Cruz B, Espinosa-Barrera L, Cardenas-Conejo Y Molecules. 2023; 28(16).

PMID: 37630332 PMC: 10458862. DOI: 10.3390/molecules28166080.


How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.

Baril S, Gose T, Schuetz J Drug Metab Dispos. 2023; 51(8):904-922.

PMID: 37438132 PMC: 10353158. DOI: 10.1124/dmd.122.001004.


References
1.
Urbatsch I, Sankaran B, Weber J, Senior A . P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem. 1995; 270(33):19383-90. DOI: 10.1074/jbc.270.33.19383. View

2.
Procko E, Ferrin-OConnell I, Ng S, Gaudet R . Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol Cell. 2006; 24(1):51-62. DOI: 10.1016/j.molcel.2006.07.034. View

3.
Otwinowski Z, Minor W . Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997; 276:307-26. DOI: 10.1016/S0076-6879(97)76066-X. View

4.
Shimizu T, Johnson K . Presteady state kinetic analysis of vanadate-induced inhibition of the dynein ATPase. J Biol Chem. 1983; 258(22):13833-40. View

5.
Khare D, Oldham M, Orelle C, Davidson A, Chen J . Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell. 2009; 33(4):528-36. PMC: 2714826. DOI: 10.1016/j.molcel.2009.01.035. View