2nrd: Difference between revisions

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[[Image:2nrd.gif|left|200px]]<br /><applet load="2nrd" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2nrd.gif|left|200px]]
caption="2nrd, resolution 2.1&Aring;" />
 
'''THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED'''<br />
{{Structure
|PDB= 2nrd |SIZE=350|CAPTION= <scene name='initialview01'>2nrd</scene>, resolution 2.1&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1]
|GENE=
}}
 
'''THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2NRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1NRD. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRD OCA].  
2NRD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. This structure supersedes the now removed PDB entry 1NRD. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRD OCA].  


==Reference==
==Reference==
The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted., Adman ET, Godden JW, Turley S, J Biol Chem. 1995 Nov 17;270(46):27458-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7499203 7499203]
The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted., Adman ET, Godden JW, Turley S, J Biol Chem. 1995 Nov 17;270(46):27458-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7499203 7499203]
[[Category: Achromobacter cycloclastes]]
[[Category: Achromobacter cycloclastes]]
[[Category: Nitrite reductase (NO-forming)]]
[[Category: Nitrite reductase (NO-forming)]]
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[[Category: oxidoreductase (nitric oxide(a))]]
[[Category: oxidoreductase (nitric oxide(a))]]


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Revision as of 18:50, 20 March 2008

File:2nrd.gif


PDB ID 2nrd

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Activity: Nitrite reductase (NO-forming), with EC number 1.7.2.1
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED


OverviewOverview

High resolution x-ray crystallographic structures of nitrite reductase from Achromobacter cycloclastes, undertaken in order to understand the pH optimum of the reaction with nitrite, show that at pH 5.0, 5.4, 6.0, 6.2, and 6.8, no significant changes occur, other than in the occupancy of the type II copper at the active site. An extensive network of hydrogen bonds, both within and between subunits of the trimer, maintains the rigidity of the protein structure. A water occupies a site approximately 1.5 A from the site of the type II copper in the structure of the type II copper-depleted structure (at pH 5.4), again with no other significant changes in structure. In nitrite-soaked crystals, nitrite binds via its oxygens to the type II copper and replaces the water normally bound to the type II copper. The active-site cavity of the protein is distinctly hydrophobic on one side and hydrophilic on the other, providing a possible path for diffusion of the product NO. Asp-98 exhibits thermal parameter values higher than its surroundings, suggesting a role in shuttling the two protons necessary for the overall reaction. The strong structural homology with cupredoxins is described.

About this StructureAbout this Structure

2NRD is a Single protein structure of sequence from Achromobacter cycloclastes. This structure supersedes the now removed PDB entry 1NRD. Full crystallographic information is available from OCA.

ReferenceReference

The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted., Adman ET, Godden JW, Turley S, J Biol Chem. 1995 Nov 17;270(46):27458-74. PMID:7499203

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