We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1fhf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fhf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1fhf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fhf| PDB=1fhf | SCENE= }}
{{STRUCTURE_1fhf| PDB=1fhf | SCENE= }}
-
'''THE STRUCTURE OF SOYBEAN PEROXIDASE'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11266599}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11266599 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11266599}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Welinder, K.]]
[[Category: Welinder, K.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:19:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:15:01 2008''

Revision as of 00:15, 1 July 2008

Image:1fhf.png

Template:STRUCTURE 1fhf

THE STRUCTURE OF SOYBEAN PEROXIDASE

Template:ABSTRACT PUBMED 11266599

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

Page seeded by OCA on Tue Jul 1 03:15:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fhf"
Personal tools