1rof
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1rof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rof" /> '''NMR STUDY OF 4FE-4S FERREDOXIN OF THERMATOGA...)
Next diff →
Revision as of 23:37, 20 November 2007
|
NMR STUDY OF 4FE-4S FERREDOXIN OF THERMATOGA MARITIMA
Overview
The solution structure of the 60-residue 1[Fe4-S4] ferredoxin from the, hyperthermophilic bacterium Thermotoga maritima was determined based on, 683 distance and 35 dihedral angle restraints that were obtained from NMR, data. In addition, data known from crystallographic studies of ferredoxins, was used for modeling of the iron-sulfur cluster and its environment. The, protein shows a globular fold very similar to the fold of the related, 1[Fe4-S4] ferredoxins from Desulfovibrio gigas and Desulfovibrio, africanus, and elements of regular secondary structure similar to those in, other ferredoxins were found in the T. maritima protein. In particular, the T. maritima protein displayed a beta-sheet structure made up of, strands located at the very NH(2) and COOH termini of the protein, and an, internal alpha-helix. The internal beta-sheet observed in the D. gigas and, D. africanus ferredoxins could not be confirmed in T. maritima ferredoxin, and is thus suggested to be only weakly present or even absent in this, protein. This result suggests that thermostability in ferredoxins is not, necessarily correlated with the content of stable elements of regular, secondary structure.
About this Structure
1ROF is a Single protein structure of sequence from Thermotoga maritima with SF4 as ligand. Full crystallographic information is available from OCA.
Reference
An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4-S4] ferredoxin., Sticht H, Wildegger G, Bentrop D, Darimont B, Sterner R, Rosch P, Eur J Biochem. 1996 May 1;237(3):726-35. PMID:8647119
Page seeded by OCA on Wed Nov 21 01:45:10 2007
