1aq8

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[[Image:1aq8.gif|left|200px]]<br /><applet load="1aq8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1aq8.gif|left|200px]]
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caption="1aq8, resolution 2.0&Aring;" />
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'''STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE REDUCED WITH ASCORBATE'''<br />
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{{Structure
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|PDB= 1aq8 |SIZE=350|CAPTION= <scene name='initialview01'>1aq8</scene>, resolution 2.0&Aring;
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|SITE= <scene name='pdbsite=CU1:Cu+Site'>CU1</scene>, <scene name='pdbsite=CU3:Cu+Site'>CU3</scene> and <scene name='pdbsite=CU5:Cu+Site'>CU5</scene>
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|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
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|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]
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|GENE=
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}}
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'''STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE REDUCED WITH ASCORBATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1AQ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=CU1:Cu+Site'>CU1</scene>, <scene name='pdbsite=CU3:Cu+Site'>CU3</scene> and <scene name='pdbsite=CU5:Cu+Site'>CU5</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ8 OCA].
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1AQ8 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=1AQ8 OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9353305 9353305]
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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]
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:55 2008''

Revision as of 08:00, 20 March 2008


PDB ID 1aq8

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites: , and
Ligands:
Activity: Transferred entry: 1.7.2.1, with EC number 1.7.99.3
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE REDUCED WITH ASCORBATE


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

1AQ8 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

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