1xme
From Proteopedia
(New page: 200px<br /><applet load="1xme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xme, resolution 2.30Å" /> '''Structure of Recombi...) |
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| - | [[Image:1xme.gif|left|200px]]<br /><applet load="1xme" size=" | + | [[Image:1xme.gif|left|200px]]<br /><applet load="1xme" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xme, resolution 2.30Å" /> | caption="1xme, resolution 2.30Å" /> | ||
'''Structure of Recombinant Cytochrome ba3 Oxidase from Thermus thermophilus'''<br /> | '''Structure of Recombinant Cytochrome ba3 Oxidase from Thermus thermophilus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome ba(3) oxidase is an integral membrane protein identified in the | + | Cytochrome ba(3) oxidase is an integral membrane protein identified in the thermophilic bacterium Thermus thermophilus. The enzyme has now been expressed recombinantly and purified with a histidine tag. As such, it crystallizes under similar conditions and in the same space group (P4(3)2(1)2) as the native protein. A novel cryoprotection scheme is described here to obtain high-resolution diffraction from these crystals, which involves soaking in a mixture of glycerol and ethylene glycol under a layer of oil. The unit-cell parameters for these crystals are larger than the native protein, apparently deriving from increased ordering of the N-terminus and an internal loop (residues 495-500) in subunit I. Hence, compared with native cytochrome ba(3) oxidase, the recombinant His-tagged protein is accommodated in an expanded but equally well ordered lattice via an alternate set of specific intermolecular contacts. The structure was refined against data to 2.3 angstroms resolution to an R factor of 21.7% and an R(free) of 23.7%. |
==About this Structure== | ==About this Structure== | ||
| - | 1XME is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with BNG, CU, HEM, HAS, CUA and GOL 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:// | + | 1XME is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=BNG:'>BNG</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=HAS:'>HAS</scene>, <scene name='pdbligand=CUA:'>CUA</scene> and <scene name='pdbligand=GOL:'>GOL</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=1XME OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
| - | [[Category: Fee, J | + | [[Category: Fee, J A.]] |
| - | [[Category: Hunsicker-Wang, L | + | [[Category: Hunsicker-Wang, L M.]] |
| - | [[Category: Pacoma, R | + | [[Category: Pacoma, R L.]] |
| - | [[Category: Stout, C | + | [[Category: Stout, C D.]] |
[[Category: BNG]] | [[Category: BNG]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:19 2008'' |
Revision as of 13:56, 21 February 2008
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Structure of Recombinant Cytochrome ba3 Oxidase from Thermus thermophilus
Overview
Cytochrome ba(3) oxidase is an integral membrane protein identified in the thermophilic bacterium Thermus thermophilus. The enzyme has now been expressed recombinantly and purified with a histidine tag. As such, it crystallizes under similar conditions and in the same space group (P4(3)2(1)2) as the native protein. A novel cryoprotection scheme is described here to obtain high-resolution diffraction from these crystals, which involves soaking in a mixture of glycerol and ethylene glycol under a layer of oil. The unit-cell parameters for these crystals are larger than the native protein, apparently deriving from increased ordering of the N-terminus and an internal loop (residues 495-500) in subunit I. Hence, compared with native cytochrome ba(3) oxidase, the recombinant His-tagged protein is accommodated in an expanded but equally well ordered lattice via an alternate set of specific intermolecular contacts. The structure was refined against data to 2.3 angstroms resolution to an R factor of 21.7% and an R(free) of 23.7%.
About this Structure
1XME is a Protein complex structure of sequences from Thermus thermophilus with , , , , and as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Full crystallographic information is available from OCA.
Reference
A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus., Hunsicker-Wang LM, Pacoma RL, Chen Y, Fee JA, Stout CD, Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):340-3. Epub 2005, Feb 24. PMID:15735345
Page seeded by OCA on Thu Feb 21 15:56:19 2008
Categories: Cytochrome-c oxidase | Protein complex | Thermus thermophilus | Chen, Y. | Fee, J A. | Hunsicker-Wang, L M. | Pacoma, R L. | Stout, C D. | BNG | CU | CUA | GOL | HAS | HEM | Cytochrome oxidase | Heme | Heme-as | Integral membrane protein
