2yxw

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[[Image:2yxw.jpg|left|200px]]<br /><applet load="2yxw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2yxw.jpg|left|200px]]
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caption="2yxw, resolution 1.50&Aring;" />
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'''The deletion mutant of Multicopper Oxidase CueO'''<br />
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{{Structure
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|PDB= 2yxw |SIZE=350|CAPTION= <scene name='initialview01'>2yxw</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> and <scene name='pdbligand=C2O:CU-O-CU LINKAGE'>C2O</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''The deletion mutant of Multicopper Oxidase CueO'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2YXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=C2O:'>C2O</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXW OCA].
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2YXW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXW OCA].
==Reference==
==Reference==
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Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site., Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T, J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17804014 17804014]
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Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site., Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T, J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17804014 17804014]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:58:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:50:16 2008''

Revision as of 16:50, 20 March 2008

Image:2yxw.jpg


PDB ID 2yxw

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



The deletion mutant of Multicopper Oxidase CueO


Overview

CueO is a multicopper oxidase (MCO) that is involved in the homeostasis of Cu in Escherichia coli and is the sole cuprous oxidase to have ever been found. Differing from other MCOs, the substrate-binding site of CueO is deeply buried under a methionine-rich helical region including alpha-helices 5, 6, and 7 that interfere with the access of organic substrates. We deleted the region Pro357-His406 and replaced it with a Gly-Gly linker. The crystal structures of a truncated mutant in the presence and in the absence of excess Cu(II) indicated that the scaffold of the CueO molecule and metal-binding sites were reserved in comparison with those of CueO. In addition, the high thermostability of the protein molecule and its spectroscopic and magnetic properties due to four Cu centers were also conserved after truncation. As for functions, the cuprous oxidase activity of the mutant was reduced to ca 10% that of recombinant CueO owing to the decrease in the affinity of the labile Cu site for Cu(I) ions, although activities for laccase substrates such as 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), p-phenylenediamine, and 2,6-dimethoxyphenol increased due to changes in the access of these organic substrates to the type I Cu site. The present engineering of CueO indicates that the methionine-rich alpha-helices function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase.

About this Structure

2YXW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site., Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T, J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:17804014

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