2ov6: Difference between revisions

Revision as of 19:51, 28 July 2008

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File:2ov6.png

Template:STRUCTURE 2ov6

The NMR structure of subunit F of the Methanogenic A1Ao ATP synthase and its interaction with the nucleotide-binding subunit BThe NMR structure of subunit F of the Methanogenic A1Ao ATP synthase and its interaction with the nucleotide-binding subunit B

Template:ABSTRACT PUBMED 17910473

About this StructureAbout this Structure

2OV6 is a Single protein structure of sequence from Methanosarcina mazei. Full experimental information is available from OCA.

ReferenceReference

NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B., Gayen S, Vivekanandan S, Biukovic G, Gruber G, Yoon HS, Biochemistry. 2007 Oct 23;46(42):11684-94. Epub 2007 Oct 2. PMID:17910473

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 {{STRUCTURE_2ov6|  PDB=2ov6  |  SCENE=  }}
-'''The NMR structure of subunit F of the Methanogenic A1Ao ATP synthase and its interaction with the nucleotide-binding subunit B'''
+===The NMR structure of subunit F of the Methanogenic A1Ao ATP synthase and its interaction with the nucleotide-binding subunit B===
-==Overview==
+<!--
-The A1AO adenosine triphosphate (ATP) synthase from archaea uses the ion gradients generated across the membrane sector (AO) to synthesize ATP in the A3B3 domain of the A1 sector. The energy coupling between the two active domains occurs via the so-called stalk part(s), to which the 12 kDa subunit F does belong. Here, we present the solution structure of the F subunit of the A1AO ATP synthase from Methanosarcina mazei Go1. Subunit F exhibits a distinct two-domain structure, with the N-terminal having 78 residues and residues 79-101 forming the flexible C-terminal part. The well-ordered N-terminal domain is composed of a four-stranded parallel beta-sheet structure and three alpha-helices placed alternately. The two domains are loosely associated with more flexibility relative to each other. The flexibility of the C-terminal domain is further confirmed by dynamics studies. In addition, the affinity of binding of mutant subunit F, with a substitution of Trp100 against Tyr and Ile at the very C-terminal end, to the nucleotide-binding subunit B was determined quantitatively using the fluorescence signals of natural subunit B (Trp430). Finally, the arrangement of subunit F within the complex is presented.
+The line below this paragraph, {{ABSTRACT_PUBMED_17910473}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17910473 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17910473}}
 ==About this Structure==
-OV6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV6 OCA].
+OV6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV6 OCA].
 ==Reference==
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 [[Category: Hydrolase]]
 [[Category: Nmr structure]]
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