1ar1: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1AR1 is a | 1AR1 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, MG, CA, HEA and LDA 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] Structure known Active Sites: CA, CUA, CUB, HM3, HMA and MM. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AR1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
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Revision as of 14:10, 5 November 2007
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STRUCTURE AT 2.7 ANGSTROM RESOLUTION OF THE PARACOCCUS DENITRIFICANS TWO-SUBUNIT CYTOCHROME C OXIDASE COMPLEXED WITH AN ANTIBODY FV FRAGMENT
OverviewOverview
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.
About this StructureAbout this Structure
1AR1 is a Protein complex structure of sequences from Mus musculus and Paracoccus denitrificans with CU, MG, CA, HEA and LDA as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Structure known Active Sites: CA, CUA, CUB, HM3, HMA and MM. Full crystallographic information is available from OCA.
ReferenceReference
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:9380672
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