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2onk

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Revision as of 07:52, 2 March 2022

ABC transporter ModBC in complex with its binding protein ModA

Structural highlights

2onk is a 10 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[WTPC_ARCFU] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system (Probable). [WTPA_ARCFU] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Binds tungstate and molybdate. [WTPB_ARCFU] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably responsible for the translocation of the substrate across the membrane (Probable).

Evolutionary Conservation

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

Publication Abstract from PubMed

ATP-binding cassette (ABC) transporter proteins carry diverse substrates across cell membranes. Whereas clinically relevant ABC exporters are implicated in various diseases or cause multidrug resistance of cancer cells, bacterial ABC importers are essential for the uptake of nutrients, including rare elements such as molybdenum. A detailed understanding of their mechanisms requires direct visualization at high resolution and in distinct conformations. Our recent structure of the multidrug ABC exporter Sav1866 has revealed an outward-facing conformation of the transmembrane domains coupled to a closed conformation of the nucleotide-binding domains, reflecting the ATP-bound state. Here we present the 3.1 A crystal structure of a putative molybdate transporter (ModB2C2) from Archaeoglobus fulgidus in complex with its binding protein (ModA). Twelve transmembrane helices of the ModB subunits provide an inward-facing conformation, with a closed gate near the external membrane boundary. The ATP-hydrolysing ModC subunits reveal a nucleotide-free, open conformation, whereas the attached binding protein aligns the substrate-binding cleft with the entrance to the presumed translocation pathway. Structural comparison of ModB2C2A with Sav1866 suggests a common alternating access and release mechanism, with binding of ATP promoting an outward-facing conformation and dissociation of the hydrolysis products promoting an inward-facing conformation.

Structure of an ABC transporter in complex with its binding protein.,Hollenstein K, Frei DC, Locher KP Nature. 2007 Mar 8;446(7132):213-6. Epub 2007 Feb 25. PMID:17322901^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hollenstein K, Frei DC, Locher KP. Structure of an ABC transporter in complex with its binding protein. Nature. 2007 Mar 8;446(7132):213-6. Epub 2007 Feb 25. PMID:17322901 doi:10.1038/nature05626

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2onk"

@@ Line 3: / Line 3: @@
 <StructureSection load='2onk' size='340' side='right'caption='[[2onk]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2onk]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ONK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2onk]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ONK FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2onk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2onk OCA], [http://pdbe.org/2onk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2onk RCSB], [http://www.ebi.ac.uk/pdbsum/2onk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2onk ProSAT]</span></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=2onk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2onk OCA], [https://pdbe.org/2onk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2onk RCSB], [https://www.ebi.ac.uk/pdbsum/2onk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2onk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/WTPC_ARCFU WTPC_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system (Probable). [[http://www.uniprot.org/uniprot/WTPA_ARCFU WTPA_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Binds tungstate and molybdate. [[http://www.uniprot.org/uniprot/WTPB_ARCFU WTPB_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably responsible for the translocation of the substrate across the membrane (Probable).
+[[https://www.uniprot.org/uniprot/WTPC_ARCFU WTPC_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system (Probable). [[https://www.uniprot.org/uniprot/WTPA_ARCFU WTPA_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Binds tungstate and molybdate. [[https://www.uniprot.org/uniprot/WTPB_ARCFU WTPB_ARCFU]] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably responsible for the translocation of the substrate across the membrane (Probable).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2onk

From Proteopedia

Revision as of 07:52, 2 March 2022

ABC transporter ModBC in complex with its binding protein ModA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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