PDBsum entry 1oxv

Transport protein

PDB id: 1oxv

Contents

Protein chains

353 a.a. *

Ligands

ANP ×3

Metals

_MG ×3

IOD ×38

Waters ×863

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Crystal structures of the atpase subunit of the glucose abc transporter from sulfolobus solfataricus: nucleotide-Free and nucleotide-Bound conformations.

Authors

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

Ref.

J Mol Biol, 2003, 330, 343-358. [DOI no: 10.1016/S0022-2836(03)00575-8]

PubMed id

12823973

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.

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.

Secondary reference #1

Title

Purification, Crystallization and preliminary X-Ray diffraction analysis of an archaeal abc-Atpase.

Authors

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

Ref.

Acta Crystallogr D Biol Crystallogr, 2002, 58, 362-365. [DOI no: 10.1107/S0907444901020765]

PubMed id

11807278

Figure 2.
Figure 2 Single orthorhombic crystal of GlcV in either form A or B: from visual inspection it is impossible to distinguish the two forms.

The above figure is reproduced from the cited reference with permission from the IUCr

Secondary reference #2

Title

Glucose transport in the extremely thermoacidophilic sulfolobus solfataricus involves a high-Affinity membrane-Integrated binding protein.

Authors

S.V.Albers, M.G.Elferink, R.L.Charlebois, C.W.Sensen, A.J.Driessen, W.N.Konings.

Ref.

J Bacteriol, 1999, 181, 4285-4291.

PubMed id

10400586