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1z53
From Proteopedia
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[[Image:1z53.gif|left|200px]] | [[Image:1z53.gif|left|200px]] | ||
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'''The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase''' | '''The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase''' | ||
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[[Category: Bhaskar, B.]] | [[Category: Bhaskar, B.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
| - | [[Category: | + | [[Category: Ccp]] |
| - | [[Category: | + | [[Category: Heme peroxidase]] |
| - | [[Category: | + | [[Category: Iron-free protoporphyrin ix]] |
| - | [[Category: | + | [[Category: Trp cation radical]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:11:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:11, 3 May 2008
The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase
Overview
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 Structure
1Z53 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 17:11:07 2008
