2e5t: Difference between revisions
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==C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP condition== | |||
<StructureSection load='2e5t' size='340' side='right'caption='[[2e5t]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2e5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5T FirstGlance]. <br> | |||
</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=2e5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5t OCA], [https://pdbe.org/2e5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5t RCSB], [https://www.ebi.ac.uk/pdbsum/2e5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPE_GEOKA ATPE_GEOKA] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/2e5t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e5t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The epsilon subunit of bacterial and chloroplast F(o)F(1)-ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound epsilon subunit from a thermophilic Bacillus PS3 at 1.9-A resolution. The C-terminal two alpha-helices were folded into a hairpin, sitting on the beta sandwich structure, as reported for Escherichia coli. A previously undescribed ATP binding motif, I(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli epsilon subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 epsilon subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the epsilon C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of F(o)F(1)-ATP synthase. | |||
Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1.,Yagi H, Kajiwara N, Tanaka H, Tsukihara T, Kato-Yamada Y, Yoshida M, Akutsu H Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11233-8. Epub 2007 Jun 20. PMID:17581881<ref>PMID:17581881</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2e5t" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[ATPase 3D structures|ATPase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Bacillus sp. | </StructureSection> | ||
[[Category: | [[Category: Bacillus sp. PS3]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Akutsu H]] | ||
[[Category: Yagi H]] | |||
Latest revision as of 21:47, 29 May 2024
C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP conditionC-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP condition
Structural highlights
FunctionATPE_GEOKA Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe epsilon subunit of bacterial and chloroplast F(o)F(1)-ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound epsilon subunit from a thermophilic Bacillus PS3 at 1.9-A resolution. The C-terminal two alpha-helices were folded into a hairpin, sitting on the beta sandwich structure, as reported for Escherichia coli. A previously undescribed ATP binding motif, I(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli epsilon subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 epsilon subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the epsilon C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of F(o)F(1)-ATP synthase. Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1.,Yagi H, Kajiwara N, Tanaka H, Tsukihara T, Kato-Yamada Y, Yoshida M, Akutsu H Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11233-8. Epub 2007 Jun 20. PMID:17581881[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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