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New page: left|200px<br /><applet load="1azr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azr, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1azr.jpg|left|200px]]<br /><applet load="1azr" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1azr.jpg|left|200px]]<br /><applet load="1azr" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1azr, resolution 2.4&Aring;" />
caption="1azr, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA ZINC AZURIN MUTANT ASP47ASP AT 2.4 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA ZINC AZURIN MUTANT ASP47ASP AT 2.4 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The Pseudomonas aeruginosa azurin mutant Asn47Asp has been isolated, its, spectroscopic and kinetic properties characterized, and the X-ray crystal, structure of its zinc derivative determined. While the optical and, electron paramagnetic resonance spectra as well as the electron-transfer, activity of the mutant are very similar to the wild-type values, the, Asn47Asp reduction potential is slightly increased by 20 mV. The mutant, crystallized in the orthorhombic space group P2(1)2(1)2(1) with cell, dimensions a = 57.8, b = 81.5 and c = 112.6 A. There are four molecules in, the asymmetric unit, packed as a tetramer which consists of two, independent dimers. The zinc site of this mutant structure is similar to, the wild-type zinc azurin and, in particular, the metal-binding site is, almost identical to the site found in the wild-type zinc-azurin structure, [Nar, Huber, Messerschmidt, Filippou, Barth, Jaquinod, Kamp &amp; Canters, (1992). Eur. J. Biochem. 205, 1123-1129]. The Asp47 side chain at that, mutation site takes on a very similar orientation to Asn47 in the, wild-type structure preserving the two hydrogen bonds with the, neighbouring Thr113 NH and O(gamma)H. Therefore, the increased reduction, potential of the mutant is probably a result of an altered charge, distribution close to the metal site.
The Pseudomonas aeruginosa azurin mutant Asn47Asp has been isolated, its spectroscopic and kinetic properties characterized, and the X-ray crystal structure of its zinc derivative determined. While the optical and electron paramagnetic resonance spectra as well as the electron-transfer activity of the mutant are very similar to the wild-type values, the Asn47Asp reduction potential is slightly increased by 20 mV. The mutant crystallized in the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 57.8, b = 81.5 and c = 112.6 A. There are four molecules in the asymmetric unit, packed as a tetramer which consists of two independent dimers. The zinc site of this mutant structure is similar to the wild-type zinc azurin and, in particular, the metal-binding site is almost identical to the site found in the wild-type zinc-azurin structure [Nar, Huber, Messerschmidt, Filippou, Barth, Jaquinod, Kamp &amp; Canters (1992). Eur. J. Biochem. 205, 1123-1129]. The Asp47 side chain at that mutation site takes on a very similar orientation to Asn47 in the wild-type structure preserving the two hydrogen bonds with the neighbouring Thr113 NH and O(gamma)H. Therefore, the increased reduction potential of the mutant is probably a result of an altered charge distribution close to the metal site.


==About this Structure==
==About this Structure==
1AZR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AZR OCA].  
1AZR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZR OCA].  


==Reference==
==Reference==
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[[Category: electron transfer(cuproprotein)]]
[[Category: electron transfer(cuproprotein)]]


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