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1nml

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[[Image:1nml.jpg|left|200px]]
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{{Seed}}
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[[Image:1nml.png|left|200px]]
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{{STRUCTURE_1nml| PDB=1nml | SCENE= }}
{{STRUCTURE_1nml| PDB=1nml | SCENE= }}
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'''Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)'''
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===Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15274917 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15274917}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:42:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:34:36 2008''

Revision as of 16:34, 27 July 2008

Image:1nml.png

Template:STRUCTURE 1nml

Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)

Template:ABSTRACT PUBMED 15274917

About this Structure

1NML is a Single protein structure of sequence from Marinobacter hydrocarbonoclasticus. 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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