1nzr: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1nzr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nzr, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
No edit summary
Line 1: Line 1:
[[Image:1nzr.gif|left|200px]]<br /><applet load="1nzr" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nzr.gif|left|200px]]<br /><applet load="1nzr" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nzr, resolution 2.2&Aring;" />
caption="1nzr, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF THE AZURIN MUTANT NICKEL-TRP48MET FROM PSEUDOMONAS AERUGINOSA AT 2.2 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE AZURIN MUTANT NICKEL-TRP48MET FROM PSEUDOMONAS AERUGINOSA AT 2.2 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The structure of the azurin mutant nickel-Trp48Met from Pseudomonas, aeruginosa has been determined by difference Fourier synthesis using, phases from the wild-type azurin model. The final crystallographic R value, is 0.170 for 17 394 reflections to a resolution of 2.2 A. The mutant, crystallized in the orthorhombic space group P2(1)2(1)2(1), a = 57.4, b =, 80.4, c = 110.3 A. The four molecules in the asymmetric unit are packed as, a dimer of dimers. The nickel metal site of this mutant structure is, similar to the zinc metal site in the azurin Asp47 mutant. The, site-specific mutation was performed at residue Trp48, which is located in, the center of the protein in a highly hydrophobic environment, to, investigate its suggested role in the long-range electron-transfer pathway, between the disulfide bond on one side of the protein to the Cu centre., The structure around the mutation site Met48 showed no significant change, compared with the wild-type structure.
The structure of the azurin mutant nickel-Trp48Met from Pseudomonas aeruginosa has been determined by difference Fourier synthesis using phases from the wild-type azurin model. The final crystallographic R value is 0.170 for 17 394 reflections to a resolution of 2.2 A. The mutant crystallized in the orthorhombic space group P2(1)2(1)2(1), a = 57.4, b = 80.4, c = 110.3 A. The four molecules in the asymmetric unit are packed as a dimer of dimers. The nickel metal site of this mutant structure is similar to the zinc metal site in the azurin Asp47 mutant. The site-specific mutation was performed at residue Trp48, which is located in the center of the protein in a highly hydrophobic environment, to investigate its suggested role in the long-range electron-transfer pathway between the disulfide bond on one side of the protein to the Cu centre. The structure around the mutation site Met48 showed no significant change compared with the wild-type structure.


==About this Structure==
==About this Structure==
1NZR 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 NI 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=1NZR OCA].  
1NZR 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=NI:'>NI</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=1NZR OCA].  


==Reference==
==Reference==
Line 15: Line 15:
[[Category: Bonander, N.]]
[[Category: Bonander, N.]]
[[Category: Hammann, C.]]
[[Category: Hammann, C.]]
[[Category: Karlsson, B.G.]]
[[Category: Karlsson, B G.]]
[[Category: Langer, V.]]
[[Category: Langer, V.]]
[[Category: Nar, H.]]
[[Category: Nar, H.]]
[[Category: Sjolin, L.]]
[[Category: Sjolin, L.]]
[[Category: Tsai, L.C.]]
[[Category: Tsai, L C.]]
[[Category: Vanngard, T.]]
[[Category: Vanngard, T.]]
[[Category: NI]]
[[Category: NI]]
Line 25: Line 25:
[[Category: electron transport (copper)]]
[[Category: electron transport (copper)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:41:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:54 2008''

Revision as of 15:11, 21 February 2008

File:1nzr.gif


1nzr, resolution 2.2Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE AZURIN MUTANT NICKEL-TRP48MET FROM PSEUDOMONAS AERUGINOSA AT 2.2 ANGSTROMS RESOLUTION

OverviewOverview

The structure of the azurin mutant nickel-Trp48Met from Pseudomonas aeruginosa has been determined by difference Fourier synthesis using phases from the wild-type azurin model. The final crystallographic R value is 0.170 for 17 394 reflections to a resolution of 2.2 A. The mutant crystallized in the orthorhombic space group P2(1)2(1)2(1), a = 57.4, b = 80.4, c = 110.3 A. The four molecules in the asymmetric unit are packed as a dimer of dimers. The nickel metal site of this mutant structure is similar to the zinc metal site in the azurin Asp47 mutant. The site-specific mutation was performed at residue Trp48, which is located in the center of the protein in a highly hydrophobic environment, to investigate its suggested role in the long-range electron-transfer pathway between the disulfide bond on one side of the protein to the Cu centre. The structure around the mutation site Met48 showed no significant change compared with the wild-type structure.

About this StructureAbout this Structure

1NZR is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the azurin mutant nickel-Trp48Met from Pseudomonas aeruginosa at 2.2 A resolution., Tsai LC, Sjolin L, Langer V, Bonander N, Karlsson BG, Vanngard T, Hammann C, Nar H, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):711-7. PMID:15299800

Page seeded by OCA on Thu Feb 21 14:11:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA