1m56

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[[Image:1m56.gif|left|200px]]<br /><applet load="1m56" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m56.gif|left|200px]]
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caption="1m56, resolution 2.3&Aring;" />
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'''Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)'''<br />
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{{Structure
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|PDB= 1m56 |SIZE=350|CAPTION= <scene name='initialview01'>1m56</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene> and <scene name='pdbligand=PEH:DI-STEAROYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEH</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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|GENE=
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}}
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'''Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1M56 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEA:'>HEA</scene> and <scene name='pdbligand=PEH:'>PEH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M56 OCA].
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1M56 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M56 OCA].
==Reference==
==Reference==
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The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12144789 12144789]
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The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12144789 12144789]
[[Category: Cytochrome-c oxidase]]
[[Category: Cytochrome-c oxidase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: membrane protein]]
[[Category: membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:00 2008''

Revision as of 10:39, 20 March 2008

Image:1m56.gif


PDB ID 1m56

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , , , and
Activity: Cytochrome-c oxidase, with EC number 1.9.3.1
Coordinates: save as pdb, mmCIF, xml



Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)


Overview

The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme.

About this Structure

1M56 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:12144789

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