1z53

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Revision as of 08:07, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1z53" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z53, resolution 1.13Å" /> '''The 1.13 Angstrom St...)
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File:1z53.gif


1z53, resolution 1.13Å

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The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase

OverviewOverview

The iron-free cytochrome c peroxidase (CCP) crystal structure has been, determined to 1.13 A and compared with the 1.2-A ferric-CCP structure., Quite unexpectedly, removal of the iron has no effect on porphyrin, geometry and distortion, indicating that protein-porphyrin interactions, and not iron coordination or formation of the axial His-Fe bond determines, porphyrin conformation. However, there are changes in solvent structure in, the distal pocket, which lead to changes in the distal His52 acid-base, catalyst. The observed ability of His52 to move in response to small, changes in solvent structure is very likely important for its role as a, catalyst in assisting in the heterolytic fission of the peroxide O-O bond.

About this StructureAbout this Structure

1Z53 is a Single protein structure of sequence from Saccharomyces cerevisiae with PP9 as ligand. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.

ReferenceReference

The 1.13-A structure of iron-free cytochrome c peroxidase., Bhaskar B, Poulos TL, J Biol Inorg Chem. 2005 Jun;10(4):425-30. Epub 2005 May 18. PMID:15900441

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