1ijp
From Proteopedia
(New page: 200px<br /><applet load="1ijp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ijp" /> '''Solution Structure of Ala20Pro/Pro64Ala subs...) |
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| - | [[Image:1ijp.jpg|left|200px]]<br /><applet load="1ijp" size=" | + | [[Image:1ijp.jpg|left|200px]]<br /><applet load="1ijp" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase'''<br /> | '''Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the A20P/P64A mutated subunit c of Escherichia coli ATP | + | The structure of the A20P/P64A mutated subunit c of Escherichia coli ATP synthase, in which the essential proline has been switched from residue 64 of the second transmembrane helix (TMH) to residue 20 of the first TMH, has been solved by (15)N,(1)H NMR in a monophasic chloroform/methanol/water (4:4:1) solvent mixture. The cA20P/P64A mutant grows as well as wild type, and the F(0)F(1) complex is fully functional in ATPase-coupled H(+) pumping. Residues 20 and 64 lie directly opposite to each other in the hairpin-like structure of wild type subunit c, and the prolinyl 64 residue is thought to induce a slight bend in TMH-2 such that it wraps around a more straightened TMH-1. In solution, the A20P/P64A substituted subunit c also forms a hairpin of two alpha-helices, with residues 41-45 forming a connecting loop as in the case of the wild type protein, but, in this case, Pro(20) induces a bend in TMH-1, which then packs against a more straightened TMH-2. The essential prolinyl residue, whether at position 64 or 20, lies close to the aspartyl 61 H(+) binding site. The prolinyl residue may introduce structural flexibility in this region of the protein, which may be necessary for the proposed movement of the alpha-helical segments during the course of the H(+) pumping catalytic cycle. |
==About this Structure== | ==About this Structure== | ||
| - | 1IJP 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:// | + | 1IJP 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=1IJP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dmitriev, O | + | [[Category: Dmitriev, O Y.]] |
| - | [[Category: Fillingame, R | + | [[Category: Fillingame, R H.]] |
[[Category: transmembrane helix]] | [[Category: transmembrane helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:32 2008'' |
Revision as of 11:12, 21 February 2008
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Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase
Overview
The structure of the A20P/P64A mutated subunit c of Escherichia coli ATP synthase, in which the essential proline has been switched from residue 64 of the second transmembrane helix (TMH) to residue 20 of the first TMH, has been solved by (15)N,(1)H NMR in a monophasic chloroform/methanol/water (4:4:1) solvent mixture. The cA20P/P64A mutant grows as well as wild type, and the F(0)F(1) complex is fully functional in ATPase-coupled H(+) pumping. Residues 20 and 64 lie directly opposite to each other in the hairpin-like structure of wild type subunit c, and the prolinyl 64 residue is thought to induce a slight bend in TMH-2 such that it wraps around a more straightened TMH-1. In solution, the A20P/P64A substituted subunit c also forms a hairpin of two alpha-helices, with residues 41-45 forming a connecting loop as in the case of the wild type protein, but, in this case, Pro(20) induces a bend in TMH-1, which then packs against a more straightened TMH-2. The essential prolinyl residue, whether at position 64 or 20, lies close to the aspartyl 61 H(+) binding site. The prolinyl residue may introduce structural flexibility in this region of the protein, which may be necessary for the proposed movement of the alpha-helical segments during the course of the H(+) pumping catalytic cycle.
About this Structure
1IJP is a Single protein structure of sequence from Escherichia coli. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices., Dmitriev OY, Fillingame RH, J Biol Chem. 2001 Jul 20;276(29):27449-54. Epub 2001 Apr 30. PMID:11331283
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