This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2cpo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cpo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2cpo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cpo| PDB=2cpo | SCENE= }}
{{STRUCTURE_2cpo| PDB=2cpo | SCENE= }}
-
'''CHLOROPEROXIDASE'''
+
===CHLOROPEROXIDASE===
-
==Overview==
+
<!--
-
BACKGROUND: Chloroperoxidase (CPO) is a versatile heme-containing enzyme that exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzyme to exhibit these multiple activities. RESULTS: Despite functional similarities with other heme enzymes, CPO folds into a novel tertiary structure dominated by eight helical segments. The catalytic base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in other peroxidases. CPO contains a hydrophobic patch above the heme that could be the binding site for substrates that undergo P450-like reactions. The crystal structure also shows extensive glycosylation with both N- and O-linked glycosyl chains. CONCLUSIONS: The proximal side of the heme in CPO resembles cytochrome P450 because a cysteine residue serves as an axial heme ligand, whereas the distal side of the heme is 'peroxidase-like' in that polar residues form the peroxide-binding site. Access to the heme pocket is restricted to the distal face such that small organic substrates can interact with the iron-linked oxygen atom which accounts for the P450-like reactions catalyzed by chloroperoxidase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8747463}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8747463 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8747463}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Haloperoxidase]]
[[Category: Haloperoxidase]]
[[Category: Heme peroxidase]]
[[Category: Heme peroxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:45:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:54:14 2008''

Revision as of 22:54, 27 July 2008

Image:2cpo.png

Template:STRUCTURE 2cpo

CHLOROPEROXIDASE

Template:ABSTRACT PUBMED 8747463

About this Structure

2CPO is a Single protein structure of sequence from Leptoxyphium fumago. Full crystallographic information is available from OCA.

Reference

The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid., Sundaramoorthy M, Terner J, Poulos TL, Structure. 1995 Dec 15;3(12):1367-77. PMID:8747463

Page seeded by OCA on Mon Jul 28 01:54:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cpo"
Personal tools