1a91: Difference between revisions

Revision as of 16:24, 30 June 2008

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File:1a91.png

Template:STRUCTURE 1a91

SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURESSUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES

Template:ABSTRACT PUBMED 9636021

About this StructureAbout this Structure

1A91 is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase., Girvin ME, Rastogi VK, Abildgaard F, Markley JL, Fillingame RH, Biochemistry. 1998 Jun 23;37(25):8817-24. PMID:9636021

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-[[Image:1a91.gif|left|200px]]
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 {{STRUCTURE_1a91|  PDB=1a91  |  SCENE=  }}
-'''SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES'''
+===SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES===
-==Overview==
+<!--
-Subunit c is the H+-translocating component of the F1F0 ATP synthase complex. H+ transport is coupled to conformational changes that ultimately lead to ATP synthesis by the enzyme. The properties of the monomeric subunit in a single-phase solution of chloroform-methanol-water (4:4:1) have been shown to mimic those of the protein in the native complex. Triple resonance NMR experiments were used to determine the complete structure of monomeric subunit c in this solvent mixture. The structure of the protein was defined by &gt;2000 interproton distances, 64 (3)JN alpha, and 43 hydrogen-bonding NMR-derived restraints. The root mean squared deviation for the backbone atoms of the two transmembrane helices was 0.63 A. The protein folds as a hairpin of two antiparallel helical segments, connected by a short structured loop. The conserved Arg41-Gln42-Pro43 form the top of this loop. The essential H+-transporting Asp61 residue is located at a slight break in the middle of the C-terminal helix, just prior to Pro64. The C-terminal helix changes direction by 30 +/- 5 degrees at the conserved Pro64. In its protonated form, the Asp61 lies in a cavity created by the absence of side chains at Gly23 and Gly27 in the N-terminal helix. The shape and charge distribution of the molecular surface of the monomeric protein suggest a packing arrangement for the oligomeric protein in the F0 complex, with the front face of one monomer packing favorably against the back face of a second monomer. The packing suggests that the proton (cation) binding site lies between packed pairs of adjacent subunit c.
+The line below this paragraph, {{ABSTRACT_PUBMED_9636021}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9636021 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9636021}}
 ==About this Structure==
-A91 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A91 OCA].
+A91 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A91 OCA].
 ==Reference==
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 [[Category: Hydrogen ion transport]]
 [[Category: Membrane protein]]
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