1ils
From Proteopedia
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|PDB= 1ils |SIZE=350|CAPTION= <scene name='initialview01'>1ils</scene>, resolution 2.2Å | |PDB= 1ils |SIZE=350|CAPTION= <scene name='initialview01'>1ils</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ils FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ils OCA], [http://www.ebi.ac.uk/pdbsum/1ils PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ils RCSB]</span> | ||
}} | }} | ||
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[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: Nar, H.]] | [[Category: Nar, H.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NO3]] | ||
[[Category: electron transfer protein]] | [[Category: electron transfer protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:29 2008'' |
Revision as of 18:21, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA
Overview
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 Structure
1ILS is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
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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