2b2s: Difference between revisions
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{{STRUCTURE_2b2s| PDB=2b2s | SCENE= }} | |||
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'''Crystal structure of an oxoferryl species of catalase-peroxidase KATG at pH7.5''' | '''Crystal structure of an oxoferryl species of catalase-peroxidase KATG at pH7.5''' | ||
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[[Category: Switala, J.]] | [[Category: Switala, J.]] | ||
[[Category: Wiseman, B.]] | [[Category: Wiseman, B.]] | ||
[[Category: | [[Category: Catalase-peroxidase]] | ||
[[Category: | [[Category: Compound i]] | ||
[[Category: | [[Category: Katg]] | ||
[[Category: | [[Category: Oxoferryl species]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:46:39 2008'' | |||
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Revision as of 16:46, 3 May 2008
Crystal structure of an oxoferryl species of catalase-peroxidase KATG at pH7.5
Overview
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.
About this Structure
2B2S 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 Sat May 3 19:46:39 2008
