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[[Image:1ar1.gif|left|200px]]


{{Structure
==Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment==
|PDB= 1ar1 |SIZE=350|CAPTION= <scene name='initialview01'>1ar1</scene>, resolution 2.7&Aring;
<StructureSection load='1ar1' size='340' side='right'caption='[[1ar1]], [[Resolution|resolution]] 2.70&Aring;' 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>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
<table><tr><td colspan='2'>[[1ar1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AR1 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ar1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ar1 OCA], [https://pdbe.org/1ar1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ar1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ar1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ar1 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ar1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ar1 OCA], [http://www.ebi.ac.uk/pdbsum/1ar1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ar1 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/COX1B_PARDE COX1B_PARDE] Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/1ar1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ar1 ConSurf].
<div style="clear:both"></div>


'''STRUCTURE AT 2.7 ANGSTROM RESOLUTION OF THE PARACOCCUS DENITRIFICANS TWO-SUBUNIT CYTOCHROME C OXIDASE COMPLEXED WITH AN ANTIBODY FV FRAGMENT'''
==See Also==
 
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The aa3 type cytochrome c oxidase consisting of the core subunits I and II only was isolated from the soil bacterium Paracoccus denitrificans and crystallized as complex with a monoclonal antibody Fv fragment. Crystals could be grown in the presence of a number of different nonionic detergents. However, only undecyl-beta-D-maltoside and cyclohexyl-hexyl-beta-D-maltoside yielded well-ordered crystals suitable for high resolution x-ray crystallographic studies. The crystals belong to space group P212121 and diffract x-rays to at least 2.5 A (1 A = 0.1 nm) resolution using synchrotron radiation. The structure was determined to a resolution of 2.7 A using molecular replacement and refined to a crystallographic R-factor of 20.5% (Rfree = 25.9%). The refined model includes subunits I and II and the 2 chains of the Fv fragment, 2 heme A molecules, 3 copper atoms, and 1 Mg/Mn atom, a new metal (Ca) binding site, 52 tentatively identified water molecules, and 9 detergent molecules. Only four of the water molecules are located in the cytoplasmic half of cytochrome c oxidase. Most of them are near the interface of subunits I and II. Several waters form a hydrogen-bonded cluster, including the heme propionates and the Mg/Mn binding site. The Fv fragment binds to the periplasmic polar domain of subunit II and is critically involved in the formation of the crystal lattice. The crystallization procedure is well reproducible and will allow for the analysis of the structures of mechanistically interesting mutant cytochrome c oxidases.
[[Category: Large Structures]]
 
==About this Structure==
1AR1 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AR1 OCA].
 
==Reference==
Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment., Ostermeier C, Harrenga A, Ermler U, Michel H, Proc Natl Acad Sci U S A. 1997 Sep 30;94(20):10547-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9380672 9380672]
[[Category: Cytochrome-c oxidase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Protein complex]]
[[Category: Ermler U]]
[[Category: Ermler, U.]]
[[Category: Harrenga A]]
[[Category: Harrenga, A.]]
[[Category: Michel H]]
[[Category: Michel, H.]]
[[Category: Ostermeier C]]
[[Category: Ostermeier, C.]]
[[Category: antibody complex]]
[[Category: complex (oxidoreductase/antibody)]]
[[Category: cytochrome oxidase]]
[[Category: electron transport]]
[[Category: transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:54 2008''

Latest revision as of 18:27, 13 March 2024

Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv FragmentStructure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment

Structural highlights

1ar1 is a 4 chain structure with sequence from Mus musculus and Paracoccus denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COX1B_PARDE Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ar1, resolution 2.70Å

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