From Proteopedia
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| | {{STRUCTURE_1b9u| PDB=1b9u | SCENE= }} | | {{STRUCTURE_1b9u| PDB=1b9u | SCENE= }} |
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| - | '''MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE'''
| + | ===MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE=== |
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| - | ==Overview==
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| - | The structure of the N-terminal transmembrane domain (residues 1-34) of subunit b of the Escherichia coli F0F1-ATP synthase has been solved by two-dimensional 1H NMR in a membrane mimetic solvent mixture of chloroform/methanol/H2O (4:4:1). Residues 4-22 form an alpha-helix, which is likely to span the hydrophobic domain of the lipid bilayer to anchor the largely hydrophilic subunit b in the membrane. The helical structure is interrupted by a rigid bend in the region of residues 23-26 with alpha-helical structure resuming at Pro-27 at an angle offset by 20 degrees from the transmembrane helix. In native subunit b, the hinge region and C-terminal alpha-helical segment would connect the transmembrane helix to the cytoplasmic domain. The transmembrane domains of the two subunit b in F0 were shown to be close to each other by cross-linking experiments in which single Cys were substituted for residues 2-21 of the native subunit and b-b dimer formation tested after oxidation with Cu(II)(phenanthroline)2. Cys residues that formed disulfide cross-links were found with a periodicity indicative of one face of an alpha-helix, over the span of residues 2-18, where Cys at positions 2, 6, and 10 formed dimers in highest yield. A model for the dimer is presented based upon the NMR structure and distance constraints from the cross-linking data. The transmembrane alpha-helices are positioned at a 23 degrees angle to each other with the side chains of Thr-6, Gln-10, Phe-14, and Phe-17 at the interface between subunits. The change in direction of helical packing at the hinge region may be important in the functional interaction of the cytoplasmic domains. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10336456}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10336456 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10336456}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1B9U is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9U OCA]. | + | 1B9U is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9U OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Atp synthase]] | | [[Category: Atp synthase]] |
| | [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:15:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:39:14 2008'' |
Revision as of 15:39, 30 June 2008
Template:STRUCTURE 1b9u
MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE
Template:ABSTRACT PUBMED 10336456
About this Structure
1B9U is a Single protein structure. Full experimental information is available from OCA.
Reference
Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase., Dmitriev O, Jones PC, Jiang W, Fillingame RH, J Biol Chem. 1999 May 28;274(22):15598-604. PMID:10336456
Page seeded by OCA on Mon Jun 30 18:39:14 2008
