1c99
From Proteopedia
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[[Image:1c99.jpg|left|200px]] | [[Image:1c99.jpg|left|200px]] | ||
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'''ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI''' | '''ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10580496 10580496] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10580496 10580496] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Girvin, M E.]] | [[Category: Girvin, M E.]] | ||
[[Category: Rastogi, V K.]] | [[Category: Rastogi, V K.]] | ||
| - | [[Category: | + | [[Category: Atp synthase]] |
| - | [[Category: | + | [[Category: Proteolipid f1fo]] |
| - | [[Category: | + | [[Category: Proton translocation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:29:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:29, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 12:29:17 2008
