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[[Image: | ==SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX== | ||
<StructureSection load='1bsh' size='340' side='right' caption='[[1bsh]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bsh]] is a 1 chain structure with 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=1BSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BSH FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bsn|1bsn]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bsh RCSB], [http://www.ebi.ac.uk/pdbsum/1bsh PDBsum]</span></td></tr> | |||
<table> | |||
== 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/bs/1bsh_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The solution structure of the epsilon subunit of the Escherichia coli F1-ATPase has been determined by NMR spectroscopy. This subunit has a two-domain structure with an N-terminal 10-stranded beta sandwich and a C-terminal antiparallel two alpha-helix hairpin, as described previously (Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. A. (1995) Nat. Struct. Biol. 2, 961-967). New data show that the two domains interact in solution in an interface formed by beta strand 7 and the very C-terminal alpha-helix. This interface involves only hydrophobic interactions. The dynamics of the epsilon subunit in solution were examined. The two domains are relatively tightly associated with little or no flexibility relative to one another. The epsilon subunit can exist in two states in the ECF1F0 complex depending on whether ATP or ADP occupies catalytic sites. Proteolysis of the epsilon subunit in solution and when bound to the core F1 complex indicates that the conformation of the polypeptide in solution closely resembles the conformation of epsilon when bound to the F1 in the ADP state. Chemical and photo-cross-linking show that the epsilon subunit spans and interacts with two beta subunits in the ADP state. These interactions are disrupted on binding of ATP + Mg2+, as is the interaction between the N- and C-terminal domains of the epsilon subunit. | |||
Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.,Wilkens S, Capaldi RA J Biol Chem. 1998 Oct 9;273(41):26645-51. PMID:9756905<ref>PMID:9756905</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[ATP synthase|ATP synthase]] | *[[ATP synthase|ATP synthase]] | ||
*[[ATPase|ATPase]] | |||
== | == References == | ||
< | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Capaldi, R A.]] | [[Category: Capaldi, R A.]] | ||
Revision as of 12:36, 13 August 2014
SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEXSOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX
Structural highlights
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 solution structure of the epsilon subunit of the Escherichia coli F1-ATPase has been determined by NMR spectroscopy. This subunit has a two-domain structure with an N-terminal 10-stranded beta sandwich and a C-terminal antiparallel two alpha-helix hairpin, as described previously (Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. A. (1995) Nat. Struct. Biol. 2, 961-967). New data show that the two domains interact in solution in an interface formed by beta strand 7 and the very C-terminal alpha-helix. This interface involves only hydrophobic interactions. The dynamics of the epsilon subunit in solution were examined. The two domains are relatively tightly associated with little or no flexibility relative to one another. The epsilon subunit can exist in two states in the ECF1F0 complex depending on whether ATP or ADP occupies catalytic sites. Proteolysis of the epsilon subunit in solution and when bound to the core F1 complex indicates that the conformation of the polypeptide in solution closely resembles the conformation of epsilon when bound to the F1 in the ADP state. Chemical and photo-cross-linking show that the epsilon subunit spans and interacts with two beta subunits in the ADP state. These interactions are disrupted on binding of ATP + Mg2+, as is the interaction between the N- and C-terminal domains of the epsilon subunit. Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.,Wilkens S, Capaldi RA J Biol Chem. 1998 Oct 9;273(41):26645-51. PMID:9756905[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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