1oxx: Difference between revisions

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New page: left|200px<br /><applet load="1oxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxx, resolution 1.45Å" /> '''Crystal structure of...
 
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[[Image:1oxx.gif|left|200px]]<br /><applet load="1oxx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1oxx, resolution 1.45&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 from Sulfolobus solfataricus energizes an ABC, transporter mediating glucose uptake. In ABC transporters, two ABC-ATPases, are believed to form a head-to-tail dimer, with both monomers contributing, conserved residues to each of the two productive active sites. In, contrast, isolated GlcV, although active, behaves apparently as a monomer, in the presence of ATP-Mg(2+), AMPPNP-Mg(2+) or ATP alone. To resolve the, oligomeric state of the active form of GlcV, we analysed the effects of, changing the putative catalytic base, residue E166, into glutamine or, alanine. Both mutants are, to different extents, defective in ATP, hydrolysis, and gel-filtration experiments revealed their dimerization in, the presence of ATP-Mg(2+). Mutant E166Q forms dimers also in the presence, of ATP alone, without Mg(2+), whereas dimerization of mutant E166A, requires both ATP and Mg(2+). These results confirm earlier reports for, other ABC-ATPases, but for the first time suggest the occurrence of a fast, equilibrium between ATP-bound monomers and ATP-bound dimers. We further, mutated two highly conserved residues of the ABC signature motif, S142 and, G144, into alanine. The G144A mutant is completely inactive and fails to, dimerize, indicating an essential role of this residue in stabilizing the, productive dimeric state. Mutant S142A retained considerable activity, and, was able to dimerize, thus implying that the interaction of the serine, with ATP is not essential for dimerization and catalysis. Furthermore, although the E166A and G144A mutants each alone are inactive, they produce, an active heterodimer, showing that disruption of one active site can be, tolerated. Our data suggest that ABC-ATPases with partially degenerated, catalytic machineries, as they occur in vivo, can still form productive, dimers to drive transport.
<StructureSection load='1oxx' size='340' side='right'caption='[[1oxx]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oxx]] is a 1 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=1OXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXX 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=1oxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxx OCA], [https://pdbe.org/1oxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxx RCSB], [https://www.ebi.ac.uk/pdbsum/1oxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxx 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/1oxx_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=1oxx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OXX 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 IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OXX OCA].
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
 
== References ==
==Reference==
<references/>
Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus., Verdon G, Albers SV, van Oosterwijk N, Dijkstra BW, Driessen AJ, Thunnissen AM, J Mol Biol. 2003 Nov 21;334(2):255-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14607117 14607117]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Sulfolobus solfataricus]]
[[Category: Large Structures]]
[[Category: Albers, S.V.]]
[[Category: Saccharolobus solfataricus]]
[[Category: Dijkstra, B.W.]]
[[Category: Albers S-V]]
[[Category: Driessen, A.J.M.]]
[[Category: Dijkstra BW]]
[[Category: Oosterwijk, N.van.]]
[[Category: Driessen AJM]]
[[Category: Thunnissen, A.M.W.H.]]
[[Category: Thunnissen AMWH]]
[[Category: Verdon, G.]]
[[Category: Verdon G]]
[[Category: IOD]]
[[Category: Van Oosterwijk N]]
[[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 01:39:41 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

1oxx is a 1 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 1.45Å
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

1oxx, resolution 1.45Å

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