1e2r

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[[Image:1e2r.gif|left|200px]]
[[Image:1e2r.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1e2r |SIZE=350|CAPTION= <scene name='initialview01'>1e2r</scene>, resolution 1.59&Aring;
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The line below this paragraph, containing "STRUCTURE_1e2r", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DHE:HEME+D'>DHE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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{{STRUCTURE_1e2r| PDB=1e2r | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2r OCA], [http://www.ebi.ac.uk/pdbsum/1e2r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e2r RCSB]</span>
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}}
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'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND'''
'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fulop, V.]]
[[Category: Fulop, V.]]
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[[Category: cyanide]]
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[[Category: Cyanide]]
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[[Category: denitrification]]
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[[Category: Denitrification]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: enzyme]]
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[[Category: Enzyme]]
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[[Category: nitrite reductase]]
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[[Category: Nitrite reductase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: periplasmic]]
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[[Category: Periplasmic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:35:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:55 2008''
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Revision as of 11:35, 2 May 2008

Image:1e2r.gif

Template:STRUCTURE 1e2r

CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND


Overview

We present a 1.59-A resolution crystal structure of reduced Paracoccus pantotrophus cytochrome cd(1) with cyanide bound to the d(1) heme and His/Met coordination of the c heme. Fe-C-N bond angles are 146 degrees for the A subunit and 164 degrees for the B subunit of the dimer. The nitrogen atom of bound cyanide is within hydrogen bonding distance of His(345) and His(388) and either a water molecule in subunit A or Tyr(25) in subunit B. The ferrous heme-cyanide complex is unusually stable (K(d) approximately 10(-6) m); we propose that this reflects both the design of the specialized d(1) heme ring and a general feature of anion reductases with active site heme. Oxidation of crystals of reduced, cyanide-bound, cytochrome cd(1) results in loss of cyanide and return to the native structure with Tyr(25) as a ligand to the d(1) heme iron and switching to His/His coordination at the c-type heme. No reason for unusually weak binding of cyanide to the ferric state can be identified; rather it is argued that the protein is designed such that a chelate-based effect drives displacement by tyrosine of cyanide or a weaker ligand, like reaction product nitric oxide, from the ferric d(1) heme.

About this Structure

1E2R is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus., Jafferji A, Allen JW, Ferguson SJ, Fulop V, J Biol Chem. 2000 Aug 18;275(33):25089-94. PMID:10827177 Page seeded by OCA on Fri May 2 14:35:14 2008

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