1hf9
From Proteopedia
(New page: 200px<br /><applet load="1hf9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hf9" /> '''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF...) |
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| - | [[Image:1hf9.jpg|left|200px]]<br /><applet load="1hf9" size=" | + | [[Image:1hf9.jpg|left|200px]]<br /><applet load="1hf9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hf9" /> | caption="1hf9" /> | ||
'''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1'''<br /> | '''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the | + | Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1HF9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1HF9 is a [http://en.wikipedia.org/wiki/Single_protein 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=1HF9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carbajo, R | + | [[Category: Carbajo, R J.]] |
| - | [[Category: Gordon-Smith, D | + | [[Category: Gordon-Smith, D J.]] |
[[Category: Neuhaus, D.]] | [[Category: Neuhaus, D.]] | ||
| - | [[Category: Runswick, M | + | [[Category: Runswick, M J.]] |
[[Category: Videler, H.]] | [[Category: Videler, H.]] | ||
| - | [[Category: Walker, J | + | [[Category: Walker, J E.]] |
| - | [[Category: Yang, J | + | [[Category: Yang, J C.]] |
[[Category: f1 atpase inhibitor]] | [[Category: f1 atpase inhibitor]] | ||
[[Category: mitochondrion]] | [[Category: mitochondrion]] | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:43 2008'' |
Revision as of 11:00, 21 February 2008
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C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1
Overview
Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.
About this Structure
1HF9 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase., Gordon-Smith DJ, Carbajo RJ, Yang JC, Videler H, Runswick MJ, Walker JE, Neuhaus D, J Mol Biol. 2001 Apr 27;308(2):325-39. PMID:11327770
Page seeded by OCA on Thu Feb 21 13:00:43 2008
