1rz6
From Proteopedia
(New page: 200px<br /><applet load="1rz6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rz6, resolution 2.20Å" /> '''Di-haem Cytochrome c...) |
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| - | [[Image:1rz6.jpg|left|200px]]<br /><applet load="1rz6" size=" | + | [[Image:1rz6.jpg|left|200px]]<br /><applet load="1rz6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rz6, resolution 2.20Å" /> | caption="1rz6, resolution 2.20Å" /> | ||
'''Di-haem Cytochrome c Peroxidase, Form IN'''<br /> | '''Di-haem Cytochrome c Peroxidase, Form IN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome c peroxidase (CCP) catalyses the reduction of H(2)O(2) to | + | Cytochrome c peroxidase (CCP) catalyses the reduction of H(2)O(2) to H(2)O, an important step in the cellular detoxification process. The crystal structure of the di-heme CCP from Pseudomonas nautica 617 was obtained in two different conformations in a redox state with the electron transfer heme reduced. Form IN, obtained at pH 4.0, does not contain Ca(2+) and was refined at 2.2 A resolution. This inactive form presents a closed conformation where the peroxidatic heme adopts a six-ligand coordination, hindering the peroxidatic reaction from taking place. Form OUT is Ca(2+) dependent and was crystallized at pH 5.3 and refined at 2.4 A resolution. This active form shows an open conformation, with release of the distal histidine (His71) ligand, providing peroxide access to the active site. This is the first time that the active and inactive states are reported for a di-heme peroxidase. |
==About this Structure== | ==About this Structure== | ||
| - | 1RZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Marinobacter_hydrocarbonoclasticus Marinobacter hydrocarbonoclasticus] with HEM and CIT 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:// | + | 1RZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Marinobacter_hydrocarbonoclasticus Marinobacter hydrocarbonoclasticus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CIT:'>CIT</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=1RZ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bonifacio, C.]] | [[Category: Bonifacio, C.]] | ||
[[Category: Bourgeois, D.]] | [[Category: Bourgeois, D.]] | ||
| - | [[Category: Dias, J | + | [[Category: Dias, J M.]] |
[[Category: Moura, I.]] | [[Category: Moura, I.]] | ||
[[Category: Pereira, A.]] | [[Category: Pereira, A.]] | ||
| - | [[Category: Romao, M | + | [[Category: Romao, M J.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:11 2008'' |
Revision as of 12:56, 21 February 2008
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Di-haem Cytochrome c Peroxidase, Form IN
Overview
Cytochrome c peroxidase (CCP) catalyses the reduction of H(2)O(2) to H(2)O, an important step in the cellular detoxification process. The crystal structure of the di-heme CCP from Pseudomonas nautica 617 was obtained in two different conformations in a redox state with the electron transfer heme reduced. Form IN, obtained at pH 4.0, does not contain Ca(2+) and was refined at 2.2 A resolution. This inactive form presents a closed conformation where the peroxidatic heme adopts a six-ligand coordination, hindering the peroxidatic reaction from taking place. Form OUT is Ca(2+) dependent and was crystallized at pH 5.3 and refined at 2.4 A resolution. This active form shows an open conformation, with release of the distal histidine (His71) ligand, providing peroxide access to the active site. This is the first time that the active and inactive states are reported for a di-heme peroxidase.
About this Structure
1RZ6 is a Single protein structure of sequence from Marinobacter hydrocarbonoclasticus with and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
Reference
Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617., Dias JM, Alves T, Bonifacio C, Pereira AS, Trincao J, Bourgeois D, Moura I, Romao MJ, Structure. 2004 Jun;12(6):961-73. PMID:15274917
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