1oxv: Difference between revisions

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New page: left|200px<br /><applet load="1oxv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxv, resolution 1.95Å" /> '''Crystal structure of...
 
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[[Image:1oxv.jpg|left|200px]]<br /><applet load="1oxv" size="450" 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==
==Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus==
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.
<StructureSection load='1oxv' size='340' side='right'caption='[[1oxv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oxv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxv OCA], [https://pdbe.org/1oxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxv RCSB], [https://www.ebi.ac.uk/pdbsum/1oxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLCV_SACS2 GLCV_SACS2] Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Responsible for energy coupling to the transport system (PubMed:12823973, PubMed:14607117). In vitro, as a free subunit, exhibits a constitutive ATPase activity (PubMed:11807278).<ref>PMID:11807278</ref> <ref>PMID:12823973</ref> <ref>PMID:14607117</ref> <ref>PMID:10400586</ref> <ref>PMID:11260467</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oxv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OXV 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].
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12823973 12823973]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Sulfolobus solfataricus]]
[[Category: Large Structures]]
[[Category: Albers, S.V.]]
[[Category: Saccharolobus solfataricus]]
[[Category: Dijkstra, B.W.]]
[[Category: Albers SV]]
[[Category: Driessen, A.J.]]
[[Category: Dijkstra BW]]
[[Category: Thunnissen, A.M.]]
[[Category: Driessen AJ]]
[[Category: Verdon, G.]]
[[Category: Thunnissen AM]]
[[Category: ANP]]
[[Category: Verdon G]]
[[Category: IOD]]
[[Category: MG]]
[[Category: abc-atpase]]
[[Category: atp-binding cassette]]
[[Category: atpase]]
[[Category: glcv]]
[[Category: sulfolobus solfataricus]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:39:19 2007''

Latest revision as of 11:03, 14 February 2024

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

Structural highlights

1oxv is a 3 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLCV_SACS2 Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Responsible for energy coupling to the transport system (PubMed:12823973, PubMed:14607117). In vitro, as a free subunit, exhibits a constitutive ATPase activity (PubMed:11807278).[1] [2] [3] [4] [5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Purification, crystallization and preliminary X-ray diffraction analysis of an archaeal ABC-ATPase. Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):362-5. PMID:11807278 doi:10.1107/s0907444901020765
  2. ↑ Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J Mol Biol. 2003 Jul 4;330(2):343-58. PMID:12823973
  3. ↑ Verdon G, Albers SV, van Oosterwijk N, Dijkstra BW, Driessen AJ, Thunnissen AM. Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus. J Mol Biol. 2003 Nov 21;334(2):255-67. PMID:14607117
  4. ↑ Albers SV, Elferink MG, Charlebois RL, Sensen CW, Driessen AJ, Konings WN. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. J Bacteriol. 1999 Jul;181(14):4285-91. PMID:10400586 doi:10.1128/JB.181.14.4285-4291.1999
  5. ↑ Elferink MG, Albers SV, Konings WN, Driessen AJ. Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol Microbiol. 2001 Mar;39(6):1494-503. PMID:11260467 doi:10.1046/j.1365-2958.2001.02336.x

1oxv, resolution 1.95Å

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