1as6: Difference between revisions
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|PDB= 1as6 |SIZE=350|CAPTION= <scene name='initialview01'>1as6</scene>, resolution 1.8Å | |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> | |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> | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/ | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1as6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1as6 OCA], [http://www.ebi.ac.uk/pdbsum/1as6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1as6 RCSB]</span> | |||
}} | }} | ||
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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] | 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: Nitrite reductase (NO-forming)]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adman, E T.]] | [[Category: Adman, E T.]] | ||
[[Category: Murphy, M E.P.]] | [[Category: Murphy, M E.P.]] | ||
[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
[[Category: copper]] | [[Category: copper]] | ||
[[Category: denitrification]] | [[Category: denitrification]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:34 2008'' | ||
Revision as of 18:46, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Nitrite reductase (NO-forming), with EC number 1.7.2.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF NITRITE BOUND TO OXIDIZED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE
OverviewOverview
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 StructureAbout this Structure
1AS6 is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.
ReferenceReference
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
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