1. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus
- Author
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Bauke W. Dijkstra, Andy-Mark W. H. Thunnissen, Arnold J. M. Driessen, Sonja V. Albers, Grégory Verdon, X-ray Crystallography, Faculty of Science and Engineering, and Molecular Microbiology
- Subjects
Models, Molecular ,MOTOR DOMAIN ,Protein Conformation ,Stereochemistry ,Molecular Sequence Data ,Static Electricity ,Allosteric regulation ,ved/biology.organism_classification_rank.species ,PROTEIN ,ATP-binding cassette transporter ,Biology ,Crystallography, X-Ray ,SEQUENCE ,Sulfolobus ,Adenosine Triphosphate ,Protein structure ,Structural Biology ,Adenine nucleotide ,Q-loop ,ABC-ATPase ,BINDING-CASSETTE ,Magnesium ,Amino Acid Sequence ,Binding site ,conformational changes ,MULTIDRUG-RESISTANCE ,Molecular Biology ,ATP-binding cassette ,X-ray crystallography ,Adenosine Triphosphatases ,Maltose transport ,Binding Sites ,Sequence Homology, Amino Acid ,Adenine Nucleotides ,ved/biology ,ACTIVE-SITE ,Sulfolobus solfataricus ,MALTOSE TRANSPORT ,HISTIDINE PERMEASE ,biology.organism_classification ,Protein Subunits ,Crystallography ,ESCHERICHIA-COLI ,ATP-Binding Cassette Transporters ,ARCHAEON THERMOCOCCUS-LITORALIS - Abstract
The ABC-ATPase GlcV energizes a binding protein-dependent ABC transporter that mediates glucose uptake in Sulfolobus solfataricus. Here, we report high-resolution crystal structures of GlcV in different states along its catalytic cycle: distinct monomeric nucleotide-free states and monomeric complexes with ADP-Mg2+ as a product-bound state, and with AMPPNP-Mg2+ as an ATP-like bound state. The structure of GlcV consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function. Comparisons of the nucleotide-free and nucleotide-bound structures of GlcV reveal re-orientations of the ABCalpha subdomain and the C-terminal domain relative to the ABCalpha/beta subdomain, and switch-like rearrangements in the P-loop and Q-loop regions. Additionally, large conformational differences are observed between the GlcV structures and those of other ABC-ATPases, further emphasizing the inherent flexibility of these proteins. Notably, a comparison of the monomeric AMPPNP-Mg2+-bound GlcV structure with that of the,dimeric ATP-Na+-bound LoID-EI71Q mutant reveals a +/-20degrees rigid body re-orientation of theABCalpha subdomain relative to the ABCalpha/beta subdomain, accompanied by a local conformational difference in the Q-loop. We propose that these differences represent conformational changes that may have a role in the mechanism of energy-transduction and/or allosteric control of the ABC-ATPase activity in bacterial importers. (C) 2003 Elsevier Science Ltd. All rights reserved.
- Published
- 2003