This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hf9
From Proteopedia
OCA (Talk | contribs)
(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...)
Next diff →
Revision as of 14:26, 20 November 2007
|
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 Tue Nov 20 16:33:56 2007
