1ehk

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[[Image:1ehk.gif|left|200px]]<br /><applet load="1ehk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ehk.gif|left|200px]]
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caption="1ehk, resolution 2.40&Aring;" />
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'''CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS'''<br />
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{{Structure
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|PDB= 1ehk |SIZE=350|CAPTION= <scene name='initialview01'>1ehk</scene>, resolution 2.40&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HAS:HEME-AS'>HAS</scene> and <scene name='pdbligand=CUA:DINUCLEAR COPPER ION'>CUA</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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'''CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EHK 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> and <scene name='pdbligand=CUA:'>CUA</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=1EHK OCA].
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1EHK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHK OCA].
==Reference==
==Reference==
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Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus., Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME, EMBO J. 2000 Apr 17;19(8):1766-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10775261 10775261]
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Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus., Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME, EMBO J. 2000 Apr 17;19(8):1766-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10775261 10775261]
[[Category: Cytochrome-c oxidase]]
[[Category: Cytochrome-c oxidase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: thermus thermophilus]]
[[Category: thermus thermophilus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:45 2008''

Revision as of 08:55, 20 March 2008

Image:1ehk.gif


PDB ID 1ehk

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: , , , and
Activity: Cytochrome-c oxidase, with EC number 1.9.3.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS


Overview

Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 A resolution using multiple anomalous dispersion (MAD) phasing and led to the discovery of a novel subunit IIa. A structure-based sequence alignment of this phylogenetically very distant oxidase with the other structurally known cytochrome oxidases leads to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases, e.g. a new electron transfer pathway leading directly from Cu(A) to Cu(B). Specific features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (O(2-), OH(-) or H(2)O) as bridging ligand at the active site and the mainly hydrophobic character of the interactions that stabilize the electron transfer complex between this oxidase and its substrate cytochrome c. New aspects of the proton pumping mechanism could be identified.

About this Structure

1EHK is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus., Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME, EMBO J. 2000 Apr 17;19(8):1766-76. PMID:10775261

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