1e2r: Difference between revisions
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'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND''' | {{Structure | ||
|PDB= 1e2r |SIZE=350|CAPTION= <scene name='initialview01'>1e2r</scene>, resolution 1.59Å | |||
|SITE= | |||
|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> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED AND CYANIDE BOUND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E2R is a [ | 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== | ||
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:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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| 1e2r, resolution 1.59Å | |||||||||||||
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| Ligands: | CYN, HEC, DHE and GOL | ||||||||||||
| 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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