1cck
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ALTERING SUBSTRATE SPECIFICITY OF CYTOCHROME C PEROXIDASE TOWARDS A SMALL MOLECULAR SUBSTRATE PEROXIDASE BY SUBSTITUTING TYROSINE FOR PHE 202
OverviewOverview
The crystal structure of recombinant pea cytosolic ascorbate peroxidase, has been refined to an R = 0.19 for data between 8.0 and 2.2 A resolution, and magnitude of F > or = 2 sigma(magnitude of F). The refined model, consists of four ascorbate peroxidase monomers consisting of 249 residues, per monomer assembled into two homodimers, with one heme group per, monomer. The ascorbate peroxidase model confirms that the pea cytosolic, enzyme is a noncovalent homodimer held together by a series of ionic, interactions arranged around the 2-fold noncrystallographic dimer axis. As, expected from the high level of sequence identity (33%), the overall fold, of the ascorbate peroxidase monomer closely resembles that of cytochrome c, peroxidase. The average root mean square differences for 137 ... [(full description)]
About this StructureAbout this Structure
1CCK is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM as [ligand]. Active as [[1]], with EC number [1.11.1.5]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:7703247
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