1jdr
From Proteopedia
(New page: 200px<br /><applet load="1jdr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdr, resolution 1.5Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1jdr.jpg|left|200px]]<br /><applet load="1jdr" size=" | + | [[Image:1jdr.jpg|left|200px]]<br /><applet load="1jdr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jdr, resolution 1.5Å" /> | caption="1jdr, resolution 1.5Å" /> | ||
'''Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase'''<br /> | '''Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Earlier work [Bonagura et al. (1996) Biochemistry 35, 6107] showed that | + | Earlier work [Bonagura et al. (1996) Biochemistry 35, 6107] showed that the K+ site found in the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (CCP). Binding of K+ at the engineered site results in a loss in activity and destabilization of the CCP compound I Trp191 cationic radical owing to long-range electrostatic effects. The engineered CCP mutant crystal structure has been refined to 1.5 A using data obtained at cryogenic temperatures which provides a more detailed basis for comparison with the naturally occurring K+ site in APX. The characteristic EPR signal associated with the Trp191 radical becomes progressively weaker as K+ is added, which correlates well with the loss in enzyme activity as [K+] is increased. These results coupled with stopped-flow studies support our earlier conclusions that the loss in activity and EPR signal is due to destabilization of the Trp191 cationic radical. |
==About this Structure== | ==About this Structure== | ||
| - | 1JDR 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 K and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1JDR 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=K:'>K</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1JDR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bhaskar, B.]] | [[Category: Bhaskar, B.]] | ||
| - | [[Category: Bonagura, C | + | [[Category: Bonagura, C A.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: Sundaramoorthy, M.]] | [[Category: Sundaramoorthy, M.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: helical bundle protein]] | [[Category: helical bundle protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:31 2008'' |
Revision as of 11:21, 21 February 2008
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Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase
Overview
Earlier work [Bonagura et al. (1996) Biochemistry 35, 6107] showed that the K+ site found in the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (CCP). Binding of K+ at the engineered site results in a loss in activity and destabilization of the CCP compound I Trp191 cationic radical owing to long-range electrostatic effects. The engineered CCP mutant crystal structure has been refined to 1.5 A using data obtained at cryogenic temperatures which provides a more detailed basis for comparison with the naturally occurring K+ site in APX. The characteristic EPR signal associated with the Trp191 radical becomes progressively weaker as K+ is added, which correlates well with the loss in enzyme activity as [K+] is increased. These results coupled with stopped-flow studies support our earlier conclusions that the loss in activity and EPR signal is due to destabilization of the Trp191 cationic radical.
About this Structure
1JDR is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
Reference
The effects of an engineered cation site on the structure, activity, and EPR properties of cytochrome c peroxidase., Bonagura CA, Sundaramoorthy M, Bhaskar B, Poulos TL, Biochemistry. 1999 Apr 27;38(17):5538-45. PMID:10220341
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