1oqb

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[[Image:1oqb.gif|left|200px]]
[[Image:1oqb.gif|left|200px]]
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{{Structure
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|PDB= 1oqb |SIZE=350|CAPTION= <scene name='initialview01'>1oqb</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1oqb", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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/Acyl-[acyl-carrier-protein]_desaturase Acyl-[acyl-carrier-protein] desaturase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.19.2 1.14.19.2] </span>
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{{STRUCTURE_1oqb| PDB=1oqb | SCENE= }}
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|RELATEDENTRY=[[1afr|1AFR]], [[1oq4|1OQ4]], [[1oq7|1OQ7]], [[1oq9|1OQ9]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqb OCA], [http://www.ebi.ac.uk/pdbsum/1oqb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oqb RCSB]</span>
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'''The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).'''
'''The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).'''
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==Reference==
==Reference==
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates., Moche M, Shanklin J, Ghoshal A, Lindqvist Y, J Biol Chem. 2003 Jul 4;278(27):25072-80. Epub 2003 Apr 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12704186 12704186]
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates., Moche M, Shanklin J, Ghoshal A, Lindqvist Y, J Biol Chem. 2003 Jul 4;278(27):25072-80. Epub 2003 Apr 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12704186 12704186]
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[[Category: Acyl-[acyl-carrier-protein] desaturase]]
 
[[Category: Ricinus communis]]
[[Category: Ricinus communis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Moche, M.]]
[[Category: Moche, M.]]
[[Category: Shanklin, J.]]
[[Category: Shanklin, J.]]
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[[Category: di-iron enzyme]]
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[[Category: Di-iron enzyme]]
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[[Category: electron transfer]]
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[[Category: Electron transfer]]
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[[Category: fatty acid biosynthesis]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: four-helix bundle]]
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[[Category: Four-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:09:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:47 2008''
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Revision as of 01:09, 3 May 2008

Template:STRUCTURE 1oqb

The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).


Overview

Delta9 stearoyl-acyl carrier protein (ACP) desaturase is a mu-oxo-bridged di-iron enzyme, which belongs to the structural class I of large helix bundle proteins and that catalyzes the NADPH and O2-dependent formation of a cis-double bond in stearoyl-ACP. The crystal structures of complexes with azide and acetate, respectively, as well as the apoand single-iron forms of Delta9 stearoyl-ACP desaturase from Ricinus communis have been determined. In the azide complex, the ligand forms a mu-1,3-bridge between the two iron ions in the active site, replacing a loosely bound water molecule. The structure of the acetate complex is similar, with acetate bridging the di-iron center in the same orientation with respect to the di-iron center. However, in this complex, the iron ligand Glu196 has changed its coordination mode from bidentate to monodentate, the first crystallographic observation of a carboxylate shift in Delta9 stearoyl-ACP desaturase. The two complexes are proposed to mimic a mu-1,2 peroxo intermediate present during catalytic turnover. There are striking structural similarities between the di-iron center in the Delta9 stearoyl-ACP desaturase-azide complex and in the reduced rubrerythrin-azide complex. This suggests that Delta9 stearoyl-ACP desaturase might catalyze the formation of water from exogenous hydrogen peroxide at a low rate. From the similarity in iron center structure, we propose that the mu-oxo-bridge in oxidized desaturase is bound to the di-iron center as in rubrerythrin and not as reported for the R2 subunit of ribonucleotide reductase and the hydroxylase subunit of methane monooxygenase. The crystal structure of the one-iron depleted desaturase species demonstrates that the affinities for the two iron ions comprising the di-iron center are not equivalent, Fe1 being the higher affinity site and Fe2 being the lower affinity site.

About this Structure

1OQB is a Single protein structure of sequence from Ricinus communis. Full crystallographic information is available from OCA.

Reference

Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates., Moche M, Shanklin J, Ghoshal A, Lindqvist Y, J Biol Chem. 2003 Jul 4;278(27):25072-80. Epub 2003 Apr 18. PMID:12704186 Page seeded by OCA on Sat May 3 04:09:19 2008

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