1as8: Difference between revisions

Revision as of 17:30, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1as8.png

Template:STRUCTURE 1as8

STRUCTURE OF NITRITE BOUND TO REDUCED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURESTRUCTURE OF NITRITE BOUND TO REDUCED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE

Template:ABSTRACT PUBMED 9353305

About this StructureAbout this Structure

1AS8 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

Page seeded by OCA on Mon Jun 30 17:30:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1as8.gif|left|200px]]
+{{Seed}}
+[[Image:1as8.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1as8|  PDB=1as8  |  SCENE=  }}
-'''STRUCTURE OF NITRITE BOUND TO REDUCED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE'''
+===STRUCTURE OF NITRITE BOUND TO REDUCED 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9353305}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9353305 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9353305}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Nitrite]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:38:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:30:28 2008''