2fqd

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(New page: 200px<br /><applet load="2fqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fqd, resolution 2.400&Aring;" /> '''Crystal Structures ...)
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'''Crystal Structures of E. coli Laccase CueO under different copper binding situations'''<br />
'''Crystal Structures of E. coli Laccase CueO under different copper binding situations'''<br />
==Overview==
==Overview==
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CueO protein is a hypothetical bacterial laccase and a good laccase, candidate for large scale industrial application. Four CueO crystal, structures were determined at different copper concentrations. Low copper, occupancy in apo-CueO and slow copper reconstitution process in CueO with, exogenous copper were demonstrated. These observations well explain the, copper dependence of CueO oxidase activity. Structural comparison between, CueO and other three fungal laccase proteins indicates that Glu106 in CueO, constitutes the primary counter-work for reconstitution of the trinuclear, copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity, and supported this hypothesis. In addition, an extra alpha-helix from, Leu351 to Gly378 covers substrate biding pocket of CueO and might, compromises the electron transfer from substrate to type I copper.
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CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.
==About this Structure==
==About this Structure==
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2FQD 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 CU, C2O and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FQD OCA].
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2FQD 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=C2O:'>C2O</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQD OCA].
==Reference==
==Reference==
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[[Category: azurin-like domain]]
[[Category: azurin-like domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:42:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:07 2008''

Revision as of 15:24, 21 February 2008

Image:2fqd.jpg

2fqd, resolution 2.400Å

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Crystal Structures of E. coli Laccase CueO under different copper binding situations

Overview

CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.

About this Structure

2FQD is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of E. coli laccase CueO at different copper concentrations., Li X, Wei Z, Zhang M, Peng X, Yu G, Teng M, Gong W, Biochem Biophys Res Commun. 2007 Mar 2;354(1):21-6. Epub 2006 Dec 22. PMID:17217912

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