1ilu
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X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA
OverviewOverview
The blue copper protein azurin from Pseudomonas aeruginosa contains a, single Trp residue that is believed to be involved in the inducible, intramolecular electron transfer from a disulphide group to the copper, centre. This residue shows in fluorescence spectra the highest energy, emission of tryptophan-containing compounds at room temperature, which is, explained by its rigid and highly hydrophobic environment. In order to, investigate the role of the Trp residue in electron transfer and the, influence of its environment, two mutations (17S and F110S) were, introduced that were thought to increase the polarity and the mobility in, its environment. The crystal structures of these mutants were solved at, 2.2 A and 2.3 A resolution, respectively. These provide a structural basis, for the changes observed in fluorescence spectra compared with the, wild-type protein. We conclude from our results that these changes are not, caused by a change in the dynamics of the Trp residue itself, but, exclusively by an increased effective dielectric constant of the, microenvironment of Trp48 and by changes in mobility of the mutated, residues.
About this StructureAbout this Structure
1ILU is a Single protein structure of sequence from Pseudomonas aeruginosa with CU as ligand. Full crystallographic information is available from OCA.
ReferenceReference
X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa., Hammann C, Messerschmidt A, Huber R, Nar H, Gilardi G, Canters GW, J Mol Biol. 1996 Jan 26;255(3):362-6. PMID:8568881
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