1fhf

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[[Image:1fhf.jpg|left|200px]]<br /><applet load="1fhf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fhf.jpg|left|200px]]
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caption="1fhf, resolution 2.80&Aring;" />
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'''THE STRUCTURE OF SOYBEAN PEROXIDASE'''<br />
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{{Structure
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|PDB= 1fhf |SIZE=350|CAPTION= <scene name='initialview01'>1fhf</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]
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|GENE=
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}}
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'''THE STRUCTURE OF SOYBEAN PEROXIDASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHF OCA].
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1FHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHF OCA].
==Reference==
==Reference==
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Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions., Henriksen A, Mirza O, Indiani C, Teilum K, Smulevich G, Welinder KG, Gajhede M, Protein Sci. 2001 Jan;10(1):108-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11266599 11266599]
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Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions., Henriksen A, Mirza O, Indiani C, Teilum K, Smulevich G, Welinder KG, Gajhede M, Protein Sci. 2001 Jan;10(1):108-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11266599 11266599]
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:11 2008''

Revision as of 09:09, 20 March 2008

Image:1fhf.jpg


PDB ID 1fhf

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: , and
Activity: Peroxidase, with EC number 1.11.1.7
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF SOYBEAN PEROXIDASE


Overview

Soybean seed coat peroxidase (SBP) is a peroxidase with extraordinary stability and catalytic properties. It belongs to the family of class III plant peroxidases that can oxidize a wide variety of organic and inorganic substrates using hydrogen peroxide. Because the plant enzyme is a heterogeneous glycoprotein, SBP was produced recombinant in Escherichia coli for the present crystallographic study. The three-dimensional structure of SBP shows a bound tris(hydroxymethyl)aminomethane molecule (TRIS). This TRIS molecule has hydrogen bonds to active site residues corresponding to the residues that interact with the small phenolic substrate ferulic acid in the horseradish peroxidase C (HRPC):ferulic acid complex. TRIS is positioned in what has been described as a secondary substrate-binding site in HRPC, and the structure of the SBP:TRIS complex indicates that this secondary substrate-binding site could be of functional importance. SBP has one of the most solvent accessible delta-meso haem edge (the site of electron transfer from reducing substrates to the enzymatic intermediates compound I and II) so far described for a plant peroxidase and structural alignment suggests that the volume of Ile74 is a factor that influences the solvent accessibility of this important site. A contact between haem C8 vinyl and the sulphur atom of Met37 is observed in the SBP structure. This interaction might affect the stability of the haem group by stabilisation/delocalisation of the porphyrin pi-cation of compound I.

About this Structure

1FHF is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions., Henriksen A, Mirza O, Indiani C, Teilum K, Smulevich G, Welinder KG, Gajhede M, Protein Sci. 2001 Jan;10(1):108-15. PMID:11266599

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