2ghh: Difference between revisions

Revision as of 04:22, 29 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:2ghh.png

Template:STRUCTURE 2ghh

Conformational mobility in the active site of a heme peroxidaseConformational mobility in the active site of a heme peroxidase

Template:ABSTRACT PUBMED 16762924

About this StructureAbout this Structure

2GHH is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:16762924

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

OCA

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-'''Conformational mobility in the active site of a heme peroxidase'''
+===Conformational mobility in the active site of a heme peroxidase===
-==Overview==
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-Conformational mobility of the distal histidine residue has been implicated for several different heme peroxidase enzymes, but unambiguous structural evidence is not available. In this work, we present mechanistic, spectroscopic, and structural evidence for peroxide- and ligand-induced conformational mobility of the distal histidine residue (His-42) in a site-directed variant of ascorbate peroxidase (W41A). In this variant, His-42 binds "on" to the heme in the oxidized form, duplicating the active site structure of the cytochromes b but, in contrast to the cytochromes b, is able to swing "off" the iron during catalysis. This conformational flexibility between the on and off forms is fully reversible and is used as a means to overcome the inherently unreactive nature of the on form toward peroxide, so that essentially complete catalytic activity is maintained. Contrary to the widely adopted view of heme enzyme catalysis, these data indicate that strong coordination of the distal histidine to the heme iron does not automatically undermine catalytic activity. The data add a new dimension to our wider appreciation of structure/activity correlations in other heme enzymes.
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