1pf3
From Proteopedia
(New page: 200px<br /><applet load="1pf3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pf3, resolution 1.50Å" /> '''Crystal Strucuture o...) |
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| - | [[Image:1pf3.jpg|left|200px]]<br /><applet load="1pf3" size=" | + | [[Image:1pf3.jpg|left|200px]]<br /><applet load="1pf3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pf3, resolution 1.50Å" /> | caption="1pf3, resolution 1.50Å" /> | ||
'''Crystal Strucuture of the M441L mutant of the multicopper oxidase CueO'''<br /> | '''Crystal Strucuture of the M441L mutant of the multicopper oxidase CueO'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CueO, a multicopper oxidase, is part of the copper-regulatory cue operon | + | CueO, a multicopper oxidase, is part of the copper-regulatory cue operon in Escherichia coli, is expressed under conditions of copper stress and shows enhanced oxidase activity when additional copper is present. The 1.7-A resolution structure of a crystal soaked in CuCl2 reveals a Cu(II) ion bound to the protein 7.5 A from the T1 copper site in a region rich in methionine residues. The trigonal bipyramidal coordination sphere is unusual, containing two methionine sulfur atoms, two aspartate carboxylate oxygen atoms, and a water molecule. Asp-439 both ligates the labile copper and hydrogen-bonds to His-443, which ligates the T1 copper. This arrangement may mediate electron transfer from substrates to the T1 copper. Mutation of residues bound to the labile copper results in loss of oxidase activity and of copper tolerance, confirming a regulatory role for this site. The methionine-rich portion of the protein, which is similar to that of other proteins involved in copper homeostasis, does not display additional copper binding. The type 3 copper atoms of the trinuclear cluster in the structure are bridged by a chloride ion that completes a square planar coordination sphere for the T2 copper atom but does not affect oxidase activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1PF3 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 and C2C as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PF3 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> and <scene name='pdbligand=C2C:'>C2C</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PF3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ambrus, A.]] | [[Category: Ambrus, A.]] | ||
[[Category: Grass, G.]] | [[Category: Grass, G.]] | ||
| - | [[Category: Montfort, W | + | [[Category: Montfort, W R.]] |
[[Category: Rensing, C.]] | [[Category: Rensing, C.]] | ||
| - | [[Category: Roberts, S | + | [[Category: Roberts, S A.]] |
[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
| - | [[Category: Wildner, G | + | [[Category: Wildner, G F.]] |
[[Category: C2C]] | [[Category: C2C]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: multicopper oxidase]] | [[Category: multicopper oxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:06 2008'' |
Revision as of 12:28, 21 February 2008
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Crystal Strucuture of the M441L mutant of the multicopper oxidase CueO
Overview
CueO, a multicopper oxidase, is part of the copper-regulatory cue operon in Escherichia coli, is expressed under conditions of copper stress and shows enhanced oxidase activity when additional copper is present. The 1.7-A resolution structure of a crystal soaked in CuCl2 reveals a Cu(II) ion bound to the protein 7.5 A from the T1 copper site in a region rich in methionine residues. The trigonal bipyramidal coordination sphere is unusual, containing two methionine sulfur atoms, two aspartate carboxylate oxygen atoms, and a water molecule. Asp-439 both ligates the labile copper and hydrogen-bonds to His-443, which ligates the T1 copper. This arrangement may mediate electron transfer from substrates to the T1 copper. Mutation of residues bound to the labile copper results in loss of oxidase activity and of copper tolerance, confirming a regulatory role for this site. The methionine-rich portion of the protein, which is similar to that of other proteins involved in copper homeostasis, does not display additional copper binding. The type 3 copper atoms of the trinuclear cluster in the structure are bridged by a chloride ion that completes a square planar coordination sphere for the T2 copper atom but does not affect oxidase activity.
About this Structure
1PF3 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO., Roberts SA, Wildner GF, Grass G, Weichsel A, Ambrus A, Rensing C, Montfort WR, J Biol Chem. 2003 Aug 22;278(34):31958-63. Epub 2003 Jun 6. PMID:12794077
Page seeded by OCA on Thu Feb 21 14:28:06 2008
Categories: Escherichia coli | Single protein | Ambrus, A. | Grass, G. | Montfort, W R. | Rensing, C. | Roberts, S A. | Weichsel, A. | Wildner, G F. | C2C | CU | Copper | Multicopper oxidase
