2ons: Difference between revisions
New page: left|200px<br /><applet load="2ons" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ons, resolution 1.55Å" /> '''Crystal structure of... |
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[[Image:2ons.gif|left|200px]]<br /><applet load="2ons" size=" | [[Image:2ons.gif|left|200px]]<br /><applet load="2ons" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ons, resolution 1.55Å" /> | caption="2ons, resolution 1.55Å" /> | ||
'''Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate'''<br /> | '''Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate'''<br /> | ||
==Overview== | ==Overview== | ||
ATP-binding cassette (ABC) transporter proteins carry diverse substrates | 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== | ==About this Structure== | ||
2ONS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with WO4, MG and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2ONS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=WO4:'>WO4</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Frei, D | [[Category: Frei, D C.]] | ||
[[Category: Hollenstein, K.]] | [[Category: Hollenstein, K.]] | ||
[[Category: Locher, K | [[Category: Locher, K P.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: NO3]] | [[Category: NO3]] | ||
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[[Category: soluble protein 2]] | [[Category: soluble protein 2]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:31 2008'' | ||
Revision as of 19:20, 21 February 2008
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Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate
OverviewOverview
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 StructureAbout this Structure
2ONS is a Single protein structure of sequence from Archaeoglobus fulgidus with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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