2vhd
From Proteopedia
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|PDB= 2vhd |SIZE=350|CAPTION= <scene name='initialview01'>2vhd</scene>, resolution 2.30Å | |PDB= 2vhd |SIZE=350|CAPTION= <scene name='initialview01'>2vhd</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Hec+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Hec+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Hec+Binding+Site+For+Chain+B'>AC5</scene> and <scene name='pdbsite=AC6:Ca+Binding+Site+For+Chain+B'>AC6</scene> | |SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Hec+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Hec+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Hec+Binding+Site+For+Chain+B'>AC5</scene> and <scene name='pdbsite=AC6:Ca+Binding+Site+For+Chain+B'>AC6</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eb7|1EB7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhd OCA], [http://www.ebi.ac.uk/pdbsum/2vhd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vhd RCSB]</span> | ||
}} | }} | ||
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[[Category: Watmough, N J.]] | [[Category: Watmough, N J.]] | ||
[[Category: Wright, J.]] | [[Category: Wright, J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEC]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 41: | Line 42: | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:18 2008'' |
Revision as of 02:12, 31 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Related: | 1EB7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PSEUDOMONAS AERUGINOSA- MIXED VALENCE FORM
Overview
A recombinant form of the prototypic diheme bacterial cytochrome c peroxidase (BCCP) from Pseudomonas aeruginosa (PsaCCP) has been expressed in Escherichia coli and purified to homogeneity. This material was used to carry out the first integrated biochemical, spectroscopic and structural investigation of the factors leading to reductive activation of this class of enzymes. A single, tightly bound, Ca2+ ion (K = 3 x 1010 M-1) found at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity. Reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis. The enzyme also forms a mixed-valence state in the absence of Ca2+ ions, but a combination of electronic absorption, and EPR spectroscopies suggests that under these circumstances the low potential heme remains six-coordinate, unable to bind substrate and therefore catalytically inactive. Our observations strongly suggest that the two mixed-valence forms of native PsaCCP reported previously by Foote and colleagues (Foote, N., Peterson, J., Gadsby, P., Greenwood, C., and Thomson, A. (1985) Biochem. J. 230, 227-237) correspond to the Ca2+-loaded and -depleted forms of the enzyme.
About this Structure
2VHD is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Redox-Linked Structural Changes Associated with the Formation of a Catalytically Competent Form of the Diheme Cytochrome c Peroxidase from Pseudomonas aeruginosa(,)., Echalier A, Brittain T, Wright J, Boycheva S, Mortuza GB, Fulop V, Watmough NJ, Biochemistry. 2008 Feb 19;47(7):1947-1956. Epub 2008 Jan 25. PMID:18217775
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