1qle
From Proteopedia
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| - | [[Image:1qle. | + | [[Image:1qle.jpg|left|200px]]<br /><applet load="1qle" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qle" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1qle, resolution 3.0Å" /> | caption="1qle, resolution 3.0Å" /> | ||
'''CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT'''<br /> | '''CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QLE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU, CA, MN, HEA, CUA and PC1 as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1QLE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb5_1.html Cytochrome c Oxidase]]. Active as [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] | + | 1QLE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU, CA, MN, HEA, CUA and PC1 as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1QLE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb5_1.html Cytochrome c Oxidase]]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:55:56 2007'' |
Revision as of 15:46, 18 December 2007
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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 with CU, CA, MN, HEA, CUA and PC1 as ligands. The following page contains interesting information on the relation of 1QLE with [Cytochrome c Oxidase]. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Known structural/functional Sites: , , , , and . 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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