|
|
| Line 1: |
Line 1: |
| [[Image:2bo5.gif|left|200px]] | | {{Seed}} |
| | [[Image:2bo5.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2bo5| PDB=2bo5 | SCENE= }} | | {{STRUCTURE_2bo5| PDB=2bo5 | SCENE= }} |
|
| |
|
| '''BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN'''
| | ===BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The peripheral stalk of ATP synthase holds the alpha3beta3 catalytic subcomplex stationary against the torque of the rotating central stalk. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha-subunits of the F1 subcomplex. Here we present the solution structure of OSCP-NT and an NMR titration study of its interaction with peptides representing N-terminal tails of F1 alpha-subunits. The structure comprises a bundle of six alpha-helices, and its interaction site contains adjoining hydrophobic surfaces of helices 1 and 5; residues in the region 1-8 of the alpha-subunit are essential for the interaction. The OSCP-NT is similar to the N-terminal domain of the delta-subunit from Escherichia coli ATP synthase (delta-NT), except that their surface charges differ (basic and acidic, respectively). As the charges of the adjacent crown regions in their alpha3beta3 complexes are similar, the OSCP-NT and delta-NT probably do not contact the crowns extensively. The N-terminal tails of alpha-subunit tails are probably alpha-helical, and so this interface, which is essential for the rotary mechanism of the enzyme, appears to consist of helix-helix interactions. | | The line below this paragraph, {{ABSTRACT_PUBMED_16045926}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16045926 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_16045926}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 2BO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. | | 2BO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. |
|
| |
|
| ==Reference== | | ==Reference== |
| Line 45: |
Line 49: |
| [[Category: Transit peptide]] | | [[Category: Transit peptide]] |
| [[Category: Transport]] | | [[Category: Transport]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:33:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:57:22 2008'' |