1hf9
From Proteopedia
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| - | [[Image:1hf9.jpg|left|200px]] | + | [[Image:1hf9.jpg|left|200px]] |
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| - | '''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1''' | + | {{Structure |
| + | |PDB= 1hf9 |SIZE=350|CAPTION= <scene name='initialview01'>1hf9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HF9 is a [ | + | 1HF9 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=1HF9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11327770 11327770] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:31 2008'' |
Revision as of 09:36, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 11:36:31 2008
