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.


1itk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1itk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1itk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1itk| PDB=1itk | SCENE= }}
{{STRUCTURE_1itk| PDB=1itk | SCENE= }}
-
'''Crystal structure of catalase-peroxidase from Haloarcula marismortui'''
+
===Crystal structure of catalase-peroxidase from Haloarcula marismortui===
-
==Overview==
+
<!--
-
Catalase-peroxidase is a member of the class I peroxidase superfamily. The enzyme exhibits both catalase and peroxidase activities to remove the harmful peroxide molecule from the living cell. The 2.0 A crystal structure of the catalase-peroxidase from Haloarcula marismortui (HmCP) reveals that the enzyme is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site of HmCP is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12172540}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12172540 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12172540}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Yamada, Y.]]
[[Category: Yamada, Y.]]
[[Category: Heme protein]]
[[Category: Heme protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:23:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:58:36 2008''

Revision as of 10:58, 1 July 2008

Image:1itk.png

Template:STRUCTURE 1itk

Crystal structure of catalase-peroxidase from Haloarcula marismortui

Template:ABSTRACT PUBMED 12172540

About this Structure

1ITK is a Single protein structure of sequence from Haloarcula marismortui. Full crystallographic information is available from OCA.

Reference

The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui., Yamada Y, Fujiwara T, Sato T, Igarashi N, Tanaka N, Nat Struct Biol. 2002 Sep;9(9):691-5. PMID:12172540

Page seeded by OCA on Tue Jul 1 13:58:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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