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1as6
From Proteopedia
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| - | [[Image:1as6.jpg|left|200px]] | + | [[Image:1as6.jpg|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF NITRITE BOUND TO OXIDIZED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE''' | + | {{Structure |
| + | |PDB= 1as6 |SIZE=350|CAPTION= <scene name='initialview01'>1as6</scene>, resolution 1.8Å | ||
| + | |SITE= <scene name='pdbsite=CU1:Cu+Site'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Site'>CU2</scene>, <scene name='pdbsite=CU3:Cu+Site'>CU3</scene>, <scene name='pdbsite=CU4:Cu+Site'>CU4</scene>, <scene name='pdbsite=CU5:Cu+Site'>CU5</scene> and <scene name='pdbsite=CU6:Cu+Site'>CU6</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=NO2:NITRITE ION'>NO2</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_1.7.2.1 Transferred entry: 1.7.2.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.3 1.7.99.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF NITRITE BOUND TO OXIDIZED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AS6 is a [ | + | 1AS6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AS6 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications., Murphy ME, Turley S, Adman ET, J Biol Chem. 1997 Nov 7;272(45):28455-60. PMID:[http:// | + | Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications., Murphy ME, Turley S, Adman ET, J Biol Chem. 1997 Nov 7;272(45):28455-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9353305 9353305] |
[[Category: Alcaligenes faecalis]] | [[Category: Alcaligenes faecalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 10:01:40 2008'' |
Revision as of 08:01, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | and | ||||||
| Activity: | Transferred entry: 1.7.2.1, with EC number 1.7.99.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF NITRITE BOUND TO OXIDIZED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE
Overview
The structures of oxidized, reduced, nitrite-soaked oxidized and nitrite-soaked reduced nitrite reductase from Alcaligenes faecalis have been determined at 1.8-2.0 A resolution using data collected at -160 degrees C. The active site at cryogenic temperature, as at room temperature, contains a tetrahedral type II copper site liganded by three histidines and a water molecule. The solvent site is empty when crystals are reduced with ascorbate. A fully occupied oxygen-coordinate nitrite occupies the solvent site in crystals soaked in nitrite. Ascorbate-reduced crystals soaked in a glycerol-methanol solution and nitrite at -40 degrees C remain colorless at -160 degrees C but turn amber-brown when warmed, suggesting that NO is released. Nitrite is found at one-half occupancy. Five new solvent sites in the oxidized nitrite bound form exhibit defined but different occupancies in the other three forms. These results support a previously proposed mechanism by which nitrite is bound primarily by a single oxygen atom that is protonable, and after reduction and cleavage of that N-O bond, NO is released leaving the oxygen atom bound to the Cu site as hydroxide or water.
About this Structure
1AS6 is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.
Reference
Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications., Murphy ME, Turley S, Adman ET, J Biol Chem. 1997 Nov 7;272(45):28455-60. PMID:9353305
Page seeded by OCA on Thu Mar 20 10:01:40 2008
