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2b2q

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{{STRUCTURE_2b2q| PDB=2b2q | SCENE= }}
{{STRUCTURE_2b2q| PDB=2b2q | SCENE= }}
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'''Crystal structure of native catalase-peroxidase KATG AT pH7.5'''
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===Crystal structure of native catalase-peroxidase KATG AT pH7.5===
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==Overview==
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The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp.
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{{ABSTRACT_PUBMED_16211084}}
==About this Structure==
==About this Structure==
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[[Category: Molecular switch]]
[[Category: Molecular switch]]
[[Category: Ph change]]
[[Category: Ph change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:55:43 2008''

Revision as of 00:55, 29 July 2008

Image:2b2q.png

Template:STRUCTURE 2b2q

Crystal structure of native catalase-peroxidase KATG AT pH7.5

Template:ABSTRACT PUBMED 16211084

About this Structure

2B2Q is a Single protein structure of sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA.

Reference

A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases., Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC, EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084

Page seeded by OCA on Tue Jul 29 03:55:43 2008

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