2ons: Difference between revisions

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-[[Image:2ons.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2ons", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2ons|  PDB=2ons  |  SCENE=  }}
-'''Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate'''
+==Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate==
+<StructureSection load='2ons' size='340' side='right'caption='[[2ons]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ons]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ONS 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]] 1.55&#8491;</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=NO3:NITRATE+ION'>NO3</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'>[https://proteopedia.org/fgij/fg.htm?mol=2ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ons OCA], [https://pdbe.org/2ons PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ons RCSB], [https://www.ebi.ac.uk/pdbsum/2ons PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ons ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== 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/on/2ons_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=2ons ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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<ref>PMID:17322901</ref>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-ONS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONS OCA].
+</div>
+<div class="pdbe-citations 2ons" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/17322901 17322901]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
-[[Category: Archaeoglobus fulgidus]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Frei, D C.]]
+__TOC__
-[[Category: Hollenstein, K.]]
+</StructureSection>
-[[Category: Locher, K P.]]
+[[Category: Archaeoglobus fulgidus DSM 4304]]
-[[Category: Soluble protein 2]]
+[[Category: Large Structures]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:17:07 2008''
+[[Category: Frei DC]]
+[[Category: Hollenstein K]]
+[[Category: Locher KP]]