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1e2r

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[[Image:1e2r.gif|left|200px]]<br /><applet load="1e2r" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e2r.gif|left|200px]]
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caption="1e2r, resolution 1.59&Aring;" />
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'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND'''<br />
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{{Structure
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|PDB= 1e2r |SIZE=350|CAPTION= <scene name='initialview01'>1e2r</scene>, resolution 1.59&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=DHE:HEME+D'>DHE</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1E2R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=CYN:'>CYN</scene>, <scene name='pdbligand=HEC:'>HEC</scene>, <scene name='pdbligand=DHE:'>DHE</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2R OCA].
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1E2R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2R OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10827177 10827177]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10827177 10827177]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: periplasmic]]
[[Category: periplasmic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:48:36 2008''

Revision as of 08:48, 20 March 2008

Image:1e2r.gif


PDB ID 1e2r

Drag the structure with the mouse to rotate
, resolution 1.59Å
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



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

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