1ils: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1ils.gif|left|200px]]
{{Seed}}
[[Image:1ils.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ils|  PDB=1ils  |  SCENE=  }}  
{{STRUCTURE_1ils|  PDB=1ils  |  SCENE=  }}  


'''X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_8568881}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8568881 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8568881}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Nar, H.]]
[[Category: Nar, H.]]
[[Category: Electron transfer protein]]
[[Category: Electron transfer protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:08:05 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:29:03 2008''

Revision as of 10:29, 1 July 2008

File:1ils.png

Template:STRUCTURE 1ils

X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA

Template:ABSTRACT PUBMED 8568881

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

Page seeded by OCA on Tue Jul 1 13:29:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ils&oldid=612459"