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1qle

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|PDB= 1qle |SIZE=350|CAPTION= <scene name='initialview01'>1qle</scene>, resolution 3.0&Aring;
|PDB= 1qle |SIZE=350|CAPTION= <scene name='initialview01'>1qle</scene>, resolution 3.0&Aring;
|SITE= <scene name='pdbsite=CA:Non+Redox+Active+Ca+Binding+Site'>CA</scene>, <scene name='pdbsite=CUA:Cu+A+Binding+Site'>CUA</scene>, <scene name='pdbsite=CUB:Cu+B+Binding+Site'>CUB</scene>, <scene name='pdbsite=HM3:Axial+Heme+A3+Ligand'>HM3</scene>, <scene name='pdbsite=HMA:Axial+Heme+A+Ligands'>HMA</scene> and <scene name='pdbsite=MM:Non+Redox+Active+Mn/Mg+Binding+Site'>MM</scene>
|SITE= <scene name='pdbsite=CA:Non+Redox+Active+Ca+Binding+Site'>CA</scene>, <scene name='pdbsite=CUA:Cu+A+Binding+Site'>CUA</scene>, <scene name='pdbsite=CUB:Cu+B+Binding+Site'>CUB</scene>, <scene name='pdbsite=HM3:Axial+Heme+A3+Ligand'>HM3</scene>, <scene name='pdbsite=HMA:Axial+Heme+A+Ligands'>HMA</scene> and <scene name='pdbsite=MM:Non+Redox+Active+Mn/Mg+Binding+Site'>MM</scene>
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene> and <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qle OCA], [http://www.ebi.ac.uk/pdbsum/1qle PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qle RCSB]</span>
}}
}}
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[[Category: Harrenga, A.]]
[[Category: Harrenga, A.]]
[[Category: Michel, H.]]
[[Category: Michel, H.]]
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[[Category: CA]]
 
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[[Category: CU]]
 
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[[Category: CUA]]
 
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[[Category: HEA]]
 
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[[Category: MN]]
 
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[[Category: PC1]]
 
[[Category: antibody complex]]
[[Category: antibody complex]]
[[Category: complex (oxidoreductase/antibody)]]
[[Category: complex (oxidoreductase/antibody)]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:24 2008''

Revision as of 20:15, 30 March 2008

Image:1qle.jpg


PDB ID 1qle

Drag the structure with the mouse to rotate
, resolution 3.0Å
Sites: , , , , and
Ligands: , , , , ,
Activity: Cytochrome-c oxidase, with EC number 1.9.3.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT


Overview

Cytochrome c oxidase catalyzes the reduction of oxygen to water. This process is accompanied by the vectorial transport of protons across the mitochondrial or bacterial membrane ("proton pumping"). The mechanism of proton pumping is still a matter of debate. Many proposed mechanisms require structural changes during the reaction cycle of cytochrome c oxidase. Therefore, the structure of the cytochrome c oxidase was determined in the completely oxidized and in the completely reduced states at a temperature of 100 K. No ligand exchanges or other major structural changes upon reduction of the cytochrome c oxidase from Paracoccus denitrificans were observed. The three histidine Cu(B) ligands are well defined in the oxidized and in the reduced states. These results are hardly compatible with the "histidine cycle" mechanisms formulated previously.

About this Structure

1QLE is a Protein complex structure of sequences from Mus musculus and Paracoccus denitrificans. The following page contains interesting information on the relation of 1QLE with [Cytochrome c Oxidase]. Full crystallographic information is available from OCA.

Reference

The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction., Harrenga A, Michel H, J Biol Chem. 1999 Nov 19;274(47):33296-9. PMID:10559205

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