2ons: Difference between revisions

Revision as of 04:44, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ons.png

Template:STRUCTURE 2ons

Crystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstateCrystal structure of A. fulgidus periplasmic binding protein ModA with bound tungstate

Template:ABSTRACT PUBMED 17322901

About this StructureAbout this Structure

2ONS is a Single protein structure of sequence from Archaeoglobus fulgidus. 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

Page seeded by OCA on Mon Jul 28 04:44:52 2008

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OCA

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-[[Image:2ons.gif|left|200px]]
+{{Seed}}
+[[Image:2ons.png|left|200px]]
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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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17322901}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17322901 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17322901}}
 ==About this Structure==
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 [[Category: Locher, K P.]]
 [[Category: Soluble protein 2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:17:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:44:52 2008''