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| [[Image:2cly.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2cly| PDB=2cly | SCENE= }} | | {{STRUCTURE_2cly| PDB=2cly | SCENE= }} |
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| '''SUBCOMPLEX OF THE STATOR OF BOVINE MITOCHONDRIAL ATP SYNTHASE'''
| | ===SUBCOMPLEX OF THE STATOR OF BOVINE MITOCHONDRIAL ATP SYNTHASE=== |
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| ==Overview==
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| The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains. | | The line below this paragraph, {{ABSTRACT_PUBMED_16791136}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16791136 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16791136}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stator]] | | [[Category: Stator]] |
| [[Category: Transport]] | | [[Category: Transport]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:27:54 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:41:23 2008'' |
