2a3t: Difference between revisions
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[[Image:2a3t.gif|left|200px]] | [[Image:2a3t.gif|left|200px]] | ||
'''Cu-containing nitrite reductase''' | {{Structure | ||
|PDB= 2a3t |SIZE=350|CAPTION= <scene name='initialview01'>2a3t</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</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= nirK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | |||
}} | |||
'''Cu-containing nitrite reductase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2A3T is a [ | 2A3T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3T OCA]. | ||
==Reference== | ==Reference== | ||
Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper., Jacobson F, Guo H, Olesen K, Okvist M, Neutze R, Sjolin L, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1190-8. Epub 2005, Aug 16. PMID:[http:// | Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper., Jacobson F, Guo H, Olesen K, Okvist M, Neutze R, Sjolin L, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1190-8. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131751 16131751] | ||
[[Category: Nitrite reductase (NO-forming)]] | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
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[[Category: nitrite reduction]] | [[Category: nitrite reduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:45:04 2008'' | ||
Revision as of 16:45, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | nirK (Rhodobacter sphaeroides) | ||||||
| Activity: | Nitrite reductase (NO-forming), with EC number 1.7.2.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cu-containing nitrite reductase
OverviewOverview
Nitrite reductase is an enzyme operating in the denitrification pathway which catalyses the conversion of nitrite (NO2(-)) to gaseous nitric oxide (NO). Here, crystal structures of the oxidized and reduced forms of the copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3 are presented at 1.74 and 1.85 A resolution, respectively. Whereas the structure of the enzyme is very similar to those of other copper-containing nitrite reductases, folding as a trimer and containing two copper sites per monomer, the structures reported here enable conformational differences between the oxidized and reduced forms of the enzyme to be identified. In the type 1 copper site, a rotational perturbation of the side chain of the copper ligand Met182 occurs upon reduction. At the type 2 copper site, a dual conformation of the catalytic residue His287 is observed in the oxidized structure but is lacking in the reduced structure, such that the interactions of the oxidized type 2 copper ion can be regarded as adopting octahedral geometry. These findings shed light on the structural mechanism of the reduction of a copper-bound nitrite to nitric oxide and water.
About this StructureAbout this Structure
2A3T is a Single protein structure of sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
ReferenceReference
Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper., Jacobson F, Guo H, Olesen K, Okvist M, Neutze R, Sjolin L, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1190-8. Epub 2005, Aug 16. PMID:16131751
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