1bsh: Difference between revisions

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[[Image:1bsh.gif|left|200px]]<br /><applet load="1bsh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bsh" />
'''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'''<br />


==Overview==
==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==
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.
<StructureSection load='1bsh' size='340' side='right'caption='[[1bsh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bsh]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1BSH 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=1bsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsh OCA], [https://pdbe.org/1bsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bsh RCSB], [https://www.ebi.ac.uk/pdbsum/1bsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPE_ECOLI ATPE_ECOLI] 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/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/main_output.php?pdb_ID=1bsh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BSH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BSH OCA].
*[[ATPase 3D structures|ATPase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9756905 9756905]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Capaldi RA]]
[[Category: Capaldi, R A.]]
[[Category: Wilkens S]]
[[Category: Wilkens, S.]]
[[Category: atpsynthase]]
[[Category: epsilon subunit]]
[[Category: f1-atpase]]
[[Category: nmr spectroscopy]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:36 2008''

Latest revision as of 18:35, 13 March 2024

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

1bsh is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATPE_ECOLI 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.

See Also

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