1oxv: Difference between revisions

Revision as of 15:22, 21 February 2008

Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus

OverviewOverview

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.

About this StructureAbout this Structure

1OXV is a Single protein structure of sequence from Sulfolobus solfataricus with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations., Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM, J Mol Biol. 2003 Jul 4;330(2):343-58. PMID:12823973

Page seeded by OCA on Thu Feb 21 14:22:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1oxv.jpg|left|200px]]<br /><applet load="1oxv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1oxv.jpg|left|200px]]<br /><applet load="1oxv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1oxv, resolution 1.95&Aring;" />
 '''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-OXV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with MG, IOD and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OXV OCA].
+OXV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXV OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Sulfolobus solfataricus]]
-[[Category: Albers, S.V.]]
+[[Category: Albers, S V.]]
-[[Category: Dijkstra, B.W.]]
+[[Category: Dijkstra, B W.]]
-[[Category: Driessen, A.J.]]
+[[Category: Driessen, A J.]]
-[[Category: Thunnissen, A.M.]]
+[[Category: Thunnissen, A M.]]
 [[Category: Verdon, G.]]
 [[Category: ANP]]
@@ Line 27: / Line 27: @@
 [[Category: sulfolobus solfataricus]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:39:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:53 2008''