1nml

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nml.jpg|left|200px]]<br /><applet load="1nml" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1nml.jpg|left|200px]]
-
caption="1nml, resolution 2.20&Aring;" />
+
 
-
'''Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)'''<br />
+
{{Structure
 +
|PDB= 1nml |SIZE=350|CAPTION= <scene name='initialview01'>1nml</scene>, resolution 2.20&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene>
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1NML 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=1NML OCA].
+
1NML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Marinobacter_hydrocarbonoclasticus Marinobacter hydrocarbonoclasticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NML OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15274917 15274917]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15274917 15274917]
[[Category: Cytochrome-c peroxidase]]
[[Category: Cytochrome-c peroxidase]]
[[Category: Marinobacter hydrocarbonoclasticus]]
[[Category: Marinobacter hydrocarbonoclasticus]]
Line 28: Line 37:
[[Category: peroxidase]]
[[Category: peroxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:46 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:52 2008''

Revision as of 10:58, 20 March 2008


PDB ID 1nml

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: and
Activity: Cytochrome-c peroxidase, with EC number 1.11.1.5
Coordinates: save as pdb, mmCIF, xml



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


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

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

Page seeded by OCA on Thu Mar 20 12:58:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools