1z53
From Proteopedia
(New page: 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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1z53.gif|left|200px]]<br /><applet load="1z53" size=" | + | [[Image:1z53.gif|left|200px]]<br /><applet load="1z53" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z53, resolution 1.13Å" /> | caption="1z53, resolution 1.13Å" /> | ||
'''The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase'''<br /> | '''The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The iron-free cytochrome c peroxidase (CCP) crystal structure has been | + | 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== | ==About this Structure== | ||
| - | 1Z53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PP9 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http:// | + | 1Z53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PP9:'>PP9</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z53 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bhaskar, B.]] | [[Category: Bhaskar, B.]] | ||
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: PP9]] | [[Category: PP9]] | ||
[[Category: ccp]] | [[Category: ccp]] | ||
| Line 22: | Line 22: | ||
[[Category: trp cation radical]] | [[Category: trp cation radical]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:11 2008'' |
Revision as of 14:12, 21 February 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 with as ligand. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 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 Thu Feb 21 16:12:11 2008
