1w2l

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[[Image:1w2l.gif|left|200px]]
[[Image:1w2l.gif|left|200px]]
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{{Structure
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|PDB= 1w2l |SIZE=350|CAPTION= <scene name='initialview01'>1w2l</scene>, resolution 1.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1w2l", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1w2l| PDB=1w2l | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2l OCA], [http://www.ebi.ac.uk/pdbsum/1w2l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w2l RCSB]</span>
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'''CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE'''
'''CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE'''
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[[Category: Srinivasan, V.]]
[[Category: Srinivasan, V.]]
[[Category: Teixeira, M.]]
[[Category: Teixeira, M.]]
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[[Category: cytochrome c domain]]
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[[Category: Cytochrome c domain]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:03:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:15 2008''
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Revision as of 10:03, 3 May 2008

Template:STRUCTURE 1w2l

CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE


Overview

The cytochrome c domain of subunit II from the Rhodothermus marinus caa(3) HiPIP:oxygen oxidoreductase, a member of the superfamily of heme-copper-containing terminal oxidases, was produced in Escherichia coli and characterised. The recombinant protein, which shows the same optical absorption and redox properties as the corresponding domain in the holo enzyme, was crystallized and its structure was determined to a resolution of 1.3 A by the multiwavelength anomalous dispersion (MAD) technique using the anomalous dispersion of the heme iron atom. The model was refined to final R(cryst) and R(free) values of 13.9% and 16.7%, respectively. The structure reveals the insertion of two short antiparallel beta-strands forming a small beta-sheet, an interesting variation of the classical all alpha-helical cytochrome c fold. This modification appears to be common to all known caa(3)-type terminal oxidases, as judged by comparative modelling and by analyses of the available amino acid sequences for these enzymes. This is the first high-resolution crystal structure reported for a cytochrome c domain of a caa(3)-type terminal oxidase. The R.marinus caa(3) uses HiPIP as the redox partner. The calculation of the electrostatic potential at the molecular surface of this extra C-terminal domain provides insights into the binding to its redox partner on one side and its interaction with the remaining subunit II on the other side.

About this Structure

1W2L is a Single protein structure of sequence from Rhodothermus marinus. Full crystallographic information is available from OCA.

Reference

Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain., Srinivasan V, Rajendran C, Sousa FL, Melo AM, Saraiva LM, Pereira MM, Santana M, Teixeira M, Michel H, J Mol Biol. 2005 Feb 4;345(5):1047-57. Epub 2004 Dec 7. PMID:15644203 Page seeded by OCA on Sat May 3 13:03:53 2008

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