2ppc

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(New page: 200px {{Structure |PDB= 2ppc |SIZE=350|CAPTION= <scene name='initialview01'>2ppc</scene>, resolution 1.58&Aring; |SITE= <scene name='pdbsite=AC1:Cu1+Binding+Site+...)
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[[Image:2ppc.jpg|left|200px]]
[[Image:2ppc.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2ppc |SIZE=350|CAPTION= <scene name='initialview01'>2ppc</scene>, resolution 1.58&Aring;
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The line below this paragraph, containing "STRUCTURE_2ppc", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cu1+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Cu+Binding+Site+For+Residue+A+502'>AC2</scene>, <scene name='pdbsite=AC3:Cu1+Binding+Site+For+Residue+B+501'>AC3</scene>, <scene name='pdbsite=AC4:Cu+Binding+Site+For+Residue+B+502'>AC4</scene>, <scene name='pdbsite=AC5:Cu1+Binding+Site+For+Residue+C+501'>AC5</scene>, <scene name='pdbsite=AC6:Cu+Binding+Site+For+Residue+C+502'>AC6</scene>, <scene name='pdbsite=AC7:No2+Binding+Site+For+Residue+A+503'>AC7</scene>, <scene name='pdbsite=AC8:No2+Binding+Site+For+Residue+B+503'>AC8</scene>, <scene name='pdbsite=AC9:Act+Binding+Site+For+Residue+B+504'>AC9</scene>, <scene name='pdbsite=BC1:No2+Binding+Site+For+Residue+C+503'>BC1</scene>, <scene name='pdbsite=BC2:Act+Binding+Site+For+Residue+C+504'>BC2</scene>, <scene name='pdbsite=BC3:Act+Binding+Site+For+Residue+B+1503'>BC3</scene>, <scene name='pdbsite=BC4:Act+Binding+Site+For+Residue+B+1504'>BC4</scene>, <scene name='pdbsite=BC5:Act+Binding+Site+For+Residue+B+1505'>BC5</scene>, <scene name='pdbsite=BC6:Act+Binding+Site+For+Residue+B+1506'>BC6</scene>, <scene name='pdbsite=BC7:Act+Binding+Site+For+Residue+C+1507'>BC7</scene>, <scene name='pdbsite=BC8:Act+Binding+Site+For+Residue+C+1508'>BC8</scene>, <scene name='pdbsite=BC9:Act+Binding+Site+For+Residue+C+1509'>BC9</scene>, <scene name='pdbsite=CC1:Act+Binding+Site+For+Residue+A+1510'>CC1</scene> and <scene name='pdbsite=CC2:Trs+Binding+Site+For+Residue+A+1501'>CC2</scene>
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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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= nirK, nir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis])
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-->
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07732 Cu-oxidase_3], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00394 Cu-oxidase]</span>
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{{STRUCTURE_2ppc| PDB=2ppc | SCENE= }}
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|RELATEDENTRY=[[1snr|1SNR]], [[1sjm|1SJM]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ppc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ppc OCA], [http://www.ebi.ac.uk/pdbsum/2ppc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ppc RCSB]</span>
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}}
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'''Oxidized wild type AfNiR exposed to NO (nitrite bound)'''
'''Oxidized wild type AfNiR exposed to NO (nitrite bound)'''
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Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17924665 17924665]
Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17924665 17924665]
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
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[[Category: Nitrite reductase (NO-forming)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Murphy, M E.P.]]
[[Category: Murphy, M E.P.]]
[[Category: Tocheva, E I.]]
[[Category: Tocheva, E I.]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: denitrification]]
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[[Category: Denitrification]]
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[[Category: nitric oxide]]
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[[Category: Nitric oxide]]
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[[Category: nitrite]]
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[[Category: Nitrite]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:34:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:57:56 2008''
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Revision as of 10:34, 4 May 2008

Image:2ppc.jpg

Template:STRUCTURE 2ppc

Oxidized wild type AfNiR exposed to NO (nitrite bound)


Overview

Nitrite reductase (NiR) is an enzyme that uses type 1 and type 2 copper sites to reduce nitrite to nitric oxide during bacterial denitrification. A copper-nitrosyl intermediate is a proposed, yet poorly characterized feature of the NiR catalytic cycle. This intermediate is formally described as Cu(I)-NO+ and is proposed to be formed at the type 2 copper site after nitrite binding and electron transfer from the type 1 copper site. In this study, copper-nitrosyl complexes were formed by prolonged exposure of exogenous NO to crystals of wild-type and two variant forms of NiR from Alcaligenes faecalis (AfNiR), and the structures were determined to 1.8 A or better resolution. Exposing oxidized wild-type crystals to NO results in the reverse reaction and formation of nitrite that remains bound at the active site. In a type 1 copper site mutant (H145A) that is incapable of electron transfer to the type 2 site, the reverse reaction is not observed. Instead, in both oxidized and reduced H145A crystals, NO is observed bound in a side-on manner to the type 2 copper. In AfNiR, Asp98 forms hydrogen bonds to both substrate and product bound to the type 2 Cu. In the D98N variant, NO is bound side-on but is more disordered when observed for the wild-type enzyme. The solution EPR spectra of the crystallographically characterized NiR-NO complexes indicate the presence of an oxidized type 2 copper site and thus are interpreted as resulting from stable copper-nitrosyls and formally assigned as Cu(II)-NO-. A reaction scheme in which a second NO molecule is oxidized to nitrite can account for the formation of a Cu(II)-NO- species after exposure of the oxidized H145A variant to NO gas.

About this Structure

2PPC is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.

Reference

Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:17924665 Page seeded by OCA on Sun May 4 13:34:56 2008

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