PDBsum entry 1oxt

Transport protein

PDB id: 1oxt

Contents

Protein chains

352 a.a. *

Waters ×647

* Residue conservation analysis

PDB id:

1oxt

Name:

Transport protein

Title:

Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus

Structure:

Abc transporter, atp binding protein. Chain: a, b, d. Synonym: glcv, glucose. Engineered: yes

Source:

Sulfolobus solfataricus. Organism_taxid: 2287. Gene: glcv. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.217 R-free: 0.275

Authors:

G.Verdon,S.V.Albers,B.W.Dijkstra,A.J.Driessen,A.M.Thunnissen

Key ref:

G.Verdon et al. (2003). Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J Mol Biol, 330, 343-358. PubMed id: 12823973 DOI: 10.1016/S0022-2836(03)00575-8

Date:

03-Apr-03 Release date: 17-Jun-03

Protein chains

Q97UY8  (Q97UY8_SULSO) -  Glucose import ATP-binding protein GlcV from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 353 a.a.

Struc: 352 a.a.

Enzyme reactions

• Enzyme class: E.C.7.5.2.- - ?????

DOI no: 10.1016/S0022-2836(03)00575-8

J Mol Biol 330:343-358 (2003)

PubMed id: 12823973

Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations.

G.Verdon, S.V.Albers, B.W.Dijkstra, A.J.Driessen, A.M.Thunnissen.

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-Mg(2+) as a product-bound state, and with AMPPNP-Mg(2+) 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-Mg(2+)-bound GlcV structure with that of the dimeric ATP-Na(+)-bound LolD-E171Q mutant reveals a +/-20 degrees rigid body re-orientation of the ABCalpha 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.

Selected figure(s)

Figure 3.
Figure 3. Stereo views of the nucleotide-binding site of GlcV in (a) nucleotide-free form A, (b) nucleotide-free form B, (c) the GlcV-ADP-Mg2+ complex and (d) the GlcV-AMPPNP-Mg2+ complex. For the complexes, a portion of a 2F[o] -F[c] simulated annealing electron density omit map[63.] is shown, contoured at 1s and covering the nucleotide, the magnesium ion and its coordinating water molecules. Residues and ligands in the nucleotide-binding site are shown in ball-and-stick representation. The P-loop is coloured in purple.

Figure 4.
Figure 4. A representation of the interactions stabilizing the nucleotide, the magnesium ion and its coordinating water molecules (red dots) in (a) the GlcV-ADP-Mg2+ complex and (b) the GlcV-AMPPNP-Mg2+ complex. Distances are in Å and residue colouring is identical with that used in Figure 1 and Figure 2.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2003, 330, 343-358) copyright 2003.

Figures were selected by an automated process.