2k6i: Difference between revisions
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==The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47== | ==The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47== | ||
<StructureSection load='2k6i' size='340' side='right'caption='[[2k6i | <StructureSection load='2k6i' size='340' side='right'caption='[[2k6i]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2k6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K6I FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k6i OCA], [https://pdbe.org/2k6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k6i RCSB], [https://www.ebi.ac.uk/pdbsum/2k6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k6i ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k6i OCA], [https://pdbe.org/2k6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k6i RCSB], [https://www.ebi.ac.uk/pdbsum/2k6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k6i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Y223_METJA Y223_METJA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: | [[Category: Biukovic G]] | ||
[[Category: | [[Category: Biukovic N]] | ||
[[Category: Gayen S]] | |||
[[Category: Gruber G]] | |||
[[Category: Pervushin K]] | |||
Latest revision as of 12:45, 9 May 2024
The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47
Structural highlights
FunctionPublication Abstract from PubMedA series of truncated forms of subunit H were generated to establish the domain features of that protein. Circular dichroism analysis demonstrated that H is divided at least into a C-terminal coiled-coil domain within residues 54-104, and an N-terminal domain formed by adjacent alpha-helices. With a cysteine at the C-terminus of each of the truncated proteins (H(1-47), H(1-54), H(1-59), H(1-61), H(1-67), H(1-69), H(1-71), H(1-78), H(1-80), H(1-91), and H(47-105)), the residues involved in formation of the coiled-coil interface were determined. Proteins H(1-54), H(1-61), H(1-69), and H(1-80) showed strong cross-link formation, which was weaker in H(1-47), H(1-59), H(1-71), and H(1-91). A shift in disulfide formation between cysteines at positions 71 and 80 reflected an interruption in the periodicity of hydrophobic residues in the region 71AEKILEETEKE81. To understand how the N-terminal domain of H is formed, we determined for the first time, to our knowledge, the solution NMR structure of H(1-47), which revealed an alpha-helix between residues 15-42 and a flexible N-terminal stretch. The alpha-helix includes a kink that would bring the two helices of the C-terminus into the coiled-coil arrangement. H(1-47) revealed a strip of alanines involved in dimerization, which were tested by exchange to single cysteines in subunit H mutants. Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47).,Biukovic G, Gayen S, Pervushin K, Gruber G Biophys J. 2009 Jul 8;97(1):286-94. PMID:19580766[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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