1pf3
From Proteopedia
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|PDB= 1pf3 |SIZE=350|CAPTION= <scene name='initialview01'>1pf3</scene>, resolution 1.50Å | |PDB= 1pf3 |SIZE=350|CAPTION= <scene name='initialview01'>1pf3</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=C2C:CU-CL-CU+LINKAGE'>C2C</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CUEO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= CUEO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kv7|1KV7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pf3 OCA], [http://www.ebi.ac.uk/pdbsum/1pf3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pf3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
[[Category: Wildner, G F.]] | [[Category: Wildner, G F.]] | ||
| - | [[Category: C2C]] | ||
| - | [[Category: CU]] | ||
[[Category: copper]] | [[Category: copper]] | ||
[[Category: multicopper oxidase]] | [[Category: multicopper oxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:47 2008'' |
Revision as of 19:58, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | CUEO (Escherichia coli) | ||||||
| Related: | 1KV7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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