1fi3
From Proteopedia
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SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551
Overview
The gene encoding for bacterial cytochrome c-551 from Pseudomonas stutzeri, substrain ZoBell has been mutated to convert the invariant sixth ligand, methionine residue into histidine, creating the site-specific mutant M61H., Proton NMR resonance assignments were made for all main-chain and, most-side chain protons in the diamagnetic, reduced form at pH 9.2 and 333, K by two-dimensional NMR techniques. Distance constraints (1074) were, determined from nuclear Overhauser enhancements and main-chain, torsion-angle constraints (72) from scalar coupling estimates. Solution, conformations for the protein were computed by the simulated annealing, approach. For 28 computed structures, the root mean squared displacement, from the average structure excluding the terminal residues 1, 2, 81, and, 82 was 0.52 A (sigma = 0.096) for backbone atoms and 0.90 A (sigma =, 0.122) for all heavy atoms. The global folding of the mutant protein is, the same as for wild type. The biggest changes are localized in a peptide, span over residues 60-65. The most striking behavior of the mutant protein, is that at room temperature and neutral pH it exists in a state similar to, the molten globular state that has been described for several proteins, under mild denaturing conditions, but the mutant converts to a more, ordered state at high pH and temperature.
About this Structure
1FI3 is a Single protein structure of sequence from Pseudomonas stutzeri with HEC as ligand. Full crystallographic information is available from OCA.
Reference
Solution conformation of the Met 61 to His 61 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551., Miller GT, Hardman JK, Timkovich R, Biophys J. 2001 Jun;80(6):2928-34. PMID:11371465
Page seeded by OCA on Tue Nov 20 14:56:23 2007
