1nib
From Proteopedia
(New page: 200px<br /><applet load="1nib" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nib, resolution 2.7Å" /> '''THE STRUCTURE OF CU-N...) |
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| - | [[Image:1nib.jpg|left|200px]]<br /><applet load="1nib" size=" | + | [[Image:1nib.jpg|left|200px]]<br /><applet load="1nib" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nib, resolution 2.7Å" /> | caption="1nib, resolution 2.7Å" /> | ||
'''THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED'''<br /> | '''THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED'''<br /> | ||
==Overview== | ==Overview== | ||
| - | High resolution x-ray crystallographic structures of nitrite reductase | + | 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 Structure== | ==About this Structure== | ||
| - | 1NIB 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 CU as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1NIB 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]. 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=1NIB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitrite reductase (NO-forming)]] | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adman, E | + | [[Category: Adman, E T.]] |
| - | [[Category: Godden, J | + | [[Category: Godden, J W.]] |
[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
[[Category: CU]] | [[Category: CU]] | ||
[[Category: oxidoreductase (nitric oxide(a))]] | [[Category: oxidoreductase (nitric oxide(a))]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:23 2008'' |
Revision as of 12:06, 21 February 2008
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THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED
Overview
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 Structure
1NIB is a Single protein structure of sequence from Achromobacter cycloclastes with as ligand. Active as Nitrite reductase (NO-forming), with EC number 1.7.2.1 Full crystallographic information is available from OCA.
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:7499203
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