1c99
From Proteopedia
(New page: 200px<br /><applet load="1c99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c99" /> '''ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE ...) |
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'''ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI'''<br /> | '''ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | F1F0 ATP synthases use a transmembrane proton gradient to drive the | + | F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 1C99 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:// | + | 1C99 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=1C99 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: Girvin, M | + | [[Category: Girvin, M E.]] |
| - | [[Category: Rastogi, V | + | [[Category: Rastogi, V K.]] |
[[Category: atp synthase]] | [[Category: atp synthase]] | ||
[[Category: proteolipid f1fo]] | [[Category: proteolipid f1fo]] | ||
[[Category: proton translocation]] | [[Category: proton translocation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:52 2008'' |
Revision as of 10:03, 21 February 2008
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ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI
Overview
F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.
About this Structure
1C99 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
Structural changes linked to proton translocation by subunit c of the ATP synthase., Rastogi VK, Girvin ME, Nature. 1999 Nov 18;402(6759):263-8. PMID:10580496
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