1eb7
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1eb7 |SIZE=350|CAPTION= <scene name='initialview01'>1eb7</scene>, resolution 2.4Å | |PDB= 1eb7 |SIZE=350|CAPTION= <scene name='initialview01'>1eb7</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=401:Low-Potential+Peroxidatic+Haem+Centre+Covalently+Linked+...'>401</scene>, <scene name='pdbsite=402:High-Potential+Haem+Centre,+Accepts+Electrons+From+Donor+...'>402</scene> and <scene name='pdbsite=403:Ca-Binding+Site,'>403</scene> | |SITE= <scene name='pdbsite=401:Low-Potential+Peroxidatic+Haem+Centre+Covalently+Linked+...'>401</scene>, <scene name='pdbsite=402:High-Potential+Haem+Centre,+Accepts+Electrons+From+Donor+...'>402</scene> and <scene name='pdbsite=403:Ca-Binding+Site,'>403</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb7 OCA], [http://www.ebi.ac.uk/pdbsum/1eb7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eb7 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEC]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 31: | Line 32: | ||
[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:06 2008'' |
Revision as of 16:59, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PSEUDOMONAS AERUGINOSA
Overview
BACKGROUND: Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis. The enzyme is located in the bacterial periplasm where its likely function is to provide protection against toxic peroxides. The soluble 323-residue single polypeptide chain contains two covalent c-type haems with very different properties: one of them is a low-potential (-330 mV) centre where hydrogen peroxide is reduced (the peroxidatic site); the other is a high-potential (+320 mV) centre which feeds electrons to the peroxidatic site from soluble electron-shuttle proteins such as cytochrome c and azurin. RESULTS: The crystal structure of the oxidized form of PsCCP has been determined to 2.4 A resolution by multiple isomorphous replacement, and refined to an R-factor of 19.2%. PsCCP is organized into two domains, both of them containing a covalent c-haem in a structure reminiscent of class 1 cytochromes c. The domains are related by a quasi-twofold axis. The domain interface holds a newly discovered calcium-binding site with an unusual set of ligands. CONCLUSIONS: The likely function of the calcium site is to maintain the structural integrity of the enzyme and/or to modulate electron transfer between the two haem domains. The low-potential haem has two histidine axial ligands (His55 and His71) and the high-potential haem is ligated by His201 and Met275. There are no polar residues at the peroxidatic site in the inactive oxidized enzyme. The structure suggests that, in the half-reduced functional form of the enzyme, the low-potential haem has to shed His71 in order to make the enzyme catalytically competent. This process is likely to trigger a reorganization of the active site, and may introduce a new residues into the haem pocket.
About this Structure
1EB7 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa., Fulop V, Ridout CJ, Greenwood C, Hajdu J, Structure. 1995 Nov 15;3(11):1225-33. PMID:8591033
Page seeded by OCA on Sun Mar 30 19:59:06 2008
