2a7u
From Proteopedia
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| - | [[Image:2a7u.gif|left|200px]] | + | [[Image:2a7u.gif|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 2a7u |SIZE=350|CAPTION= <scene name='initialview01'>2a7u</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= atpH, papE, uncH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A7U is a [ | + | 2A7U is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 2A7U with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb72_1.html ATP Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7U OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16128580 16128580] |
[[Category: ATP Synthase]] | [[Category: ATP Synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: alpha helix bundle]] | [[Category: alpha helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:32 2008'' |
Revision as of 13:46, 20 March 2008
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| Gene: | atpH, papE, uncH (Escherichia coli) | ||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues
Overview
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.
About this Structure
2A7U is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 2A7U with [ATP Synthase]. Full crystallographic information is available from OCA.
Reference
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
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