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==NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues==
==NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues==
<StructureSection load='2a7u' size='340' side='right'caption='[[2a7u]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='2a7u' size='340' side='right'caption='[[2a7u]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2a7u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. The December 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7U FirstGlance]. <br>
<table><tr><td colspan='2'>[[2a7u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. The December 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7U FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1abv|1abv]]</div></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpH, papE, uncH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </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=2a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7u OCA], [https://pdbe.org/2a7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7u RCSB], [https://www.ebi.ac.uk/pdbsum/2a7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7u 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=2a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7u OCA], [https://pdbe.org/2a7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7u RCSB], [https://www.ebi.ac.uk/pdbsum/2a7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ATPA_ECOLI ATPA_ECOLI]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] [[https://www.uniprot.org/uniprot/ATPD_ECOLI ATPD_ECOLI]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01416]  This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416]
[https://www.uniprot.org/uniprot/ATPA_ECO57 ATPA_ECO57] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2a7u ConSurf].
</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=2a7u ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A critical point of interaction between F(1) and F(0) in the bacterial F(1)F(0)-ATP synthase is formed by the alpha and delta subunits. Previous work has shown that the N-terminal domain (residues 3-105) of the delta subunit forms a 6 alpha-helix bundle [Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W., and Capaldi, R. A. (1997) Nat. Struct. Biol. 4, 198-201] and that the majority of the binding energy between delta and F(1) is provided by the interaction between the N-terminal 22 residues of the alpha- and N-terminal domain of the delta subunit [Weber, J., Muharemagic, A., Wilke-Mounts, S., and Senior, A. E. (2003) J. Biol. Chem. 278, 13623-13626]. We have now analyzed a 1:1 complex of the delta-subunit N-terminal domain and a peptide comprising the N-terminal 22 residues of the alpha subunit by heteronuclear protein NMR spectroscopy. A comparison of the chemical-shift values of delta-subunit residues with and without alpha N-terminal peptide bound indicates that the binding interface on the N-terminal domain of the delta subunit is formed by alpha helices I and V. NOE cross-peak patterns in 2D (12)C/(12)C-filtered NOESY spectra of the (13)C-labeled delta-subunit N-terminal domain in complex with unlabeled peptide verify that residues 8-18 in the alpha-subunit N-terminal peptide are folded as an alpha helix when bound to delta N-terminal domain. On the basis of intermolecular contacts observed in (12)C/(13)C-filtered NOESY experiments, we describe structural details of the interaction of the delta-subunit N-terminal domain with the alpha-subunit N-terminal alpha helix.
Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.,Wilkens S, Borchardt D, Weber J, Senior AE Biochemistry. 2005 Sep 6;44(35):11786-94. PMID:16128580<ref>PMID:16128580</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2a7u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: ATP Synthase]]
[[Category: ATP Synthase]]
[[Category: Eco57]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Borchardt, D]]
[[Category: Borchardt D]]
[[Category: Senior, A E]]
[[Category: Senior AE]]
[[Category: Weber, J]]
[[Category: Weber J]]
[[Category: Wilkens, S]]
[[Category: Wilkens S]]
[[Category: Alpha helix bundle]]
[[Category: Hydrolase]]

Latest revision as of 09:37, 1 May 2024

NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residuesNMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues

Structural highlights

2a7u is a 2 chain structure with sequence from Escherichia coli and Escherichia coli O157:H7. The December 2005 RCSB PDB Molecule of the Month feature on ATP Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_12. 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

ATPA_ECO57 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

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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