1itk: Difference between revisions

Revision as of 13:58, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1itk.png

Template:STRUCTURE 1itk

Crystal structure of catalase-peroxidase from Haloarcula marismortuiCrystal structure of catalase-peroxidase from Haloarcula marismortui

Template:ABSTRACT PUBMED 12172540

About this StructureAbout this Structure

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

ReferenceReference

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?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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.
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+{{ABSTRACT_PUBMED_12172540}}
 ==About this Structure==
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 [[Category: Yamada, Y.]]
 [[Category: Heme protein]]
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