1a91
From Proteopedia
(New page: 200px<br /><applet load="1a91" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a91" /> '''SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHER...) |
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'''SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES'''<br /> | '''SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Subunit c is the H+-translocating component of the F1F0 ATP synthase | + | Subunit c is the H+-translocating component of the F1F0 ATP synthase complex. H+ transport is coupled to conformational changes that ultimately lead to ATP synthesis by the enzyme. The properties of the monomeric subunit in a single-phase solution of chloroform-methanol-water (4:4:1) have been shown to mimic those of the protein in the native complex. Triple resonance NMR experiments were used to determine the complete structure of monomeric subunit c in this solvent mixture. The structure of the protein was defined by >2000 interproton distances, 64 (3)JN alpha, and 43 hydrogen-bonding NMR-derived restraints. The root mean squared deviation for the backbone atoms of the two transmembrane helices was 0.63 A. The protein folds as a hairpin of two antiparallel helical segments, connected by a short structured loop. The conserved Arg41-Gln42-Pro43 form the top of this loop. The essential H+-transporting Asp61 residue is located at a slight break in the middle of the C-terminal helix, just prior to Pro64. The C-terminal helix changes direction by 30 +/- 5 degrees at the conserved Pro64. In its protonated form, the Asp61 lies in a cavity created by the absence of side chains at Gly23 and Gly27 in the N-terminal helix. The shape and charge distribution of the molecular surface of the monomeric protein suggest a packing arrangement for the oligomeric protein in the F0 complex, with the front face of one monomer packing favorably against the back face of a second monomer. The packing suggests that the proton (cation) binding site lies between packed pairs of adjacent subunit c. |
==About this Structure== | ==About this Structure== | ||
| - | 1A91 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:// | + | 1A91 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=1A91 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Abildgaard, F.]] | [[Category: Abildgaard, F.]] | ||
| - | [[Category: Fillingame, R | + | [[Category: Fillingame, R H.]] |
| - | [[Category: Girvin, M | + | [[Category: Girvin, M E.]] |
| - | [[Category: Markley, J | + | [[Category: Markley, J L.]] |
| - | [[Category: Rastogi, V | + | [[Category: Rastogi, V K.]] |
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:12 2008'' |
Revision as of 09:42, 21 February 2008
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SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES
Overview
Subunit c is the H+-translocating component of the F1F0 ATP synthase complex. H+ transport is coupled to conformational changes that ultimately lead to ATP synthesis by the enzyme. The properties of the monomeric subunit in a single-phase solution of chloroform-methanol-water (4:4:1) have been shown to mimic those of the protein in the native complex. Triple resonance NMR experiments were used to determine the complete structure of monomeric subunit c in this solvent mixture. The structure of the protein was defined by >2000 interproton distances, 64 (3)JN alpha, and 43 hydrogen-bonding NMR-derived restraints. The root mean squared deviation for the backbone atoms of the two transmembrane helices was 0.63 A. The protein folds as a hairpin of two antiparallel helical segments, connected by a short structured loop. The conserved Arg41-Gln42-Pro43 form the top of this loop. The essential H+-transporting Asp61 residue is located at a slight break in the middle of the C-terminal helix, just prior to Pro64. The C-terminal helix changes direction by 30 +/- 5 degrees at the conserved Pro64. In its protonated form, the Asp61 lies in a cavity created by the absence of side chains at Gly23 and Gly27 in the N-terminal helix. The shape and charge distribution of the molecular surface of the monomeric protein suggest a packing arrangement for the oligomeric protein in the F0 complex, with the front face of one monomer packing favorably against the back face of a second monomer. The packing suggests that the proton (cation) binding site lies between packed pairs of adjacent subunit c.
About this Structure
1A91 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
Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase., Girvin ME, Rastogi VK, Abildgaard F, Markley JL, Fillingame RH, Biochemistry. 1998 Jun 23;37(25):8817-24. PMID:9636021
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