An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE

Helland, Ronny, Fjellbirkeland, Anne, Karlsen, Odd Andre, Ve, Thomas, Lillehaug, Johan R. and Jensen, Harald B. (2008) An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE. Journal of Biological Chemistry, 283 20: 13897-13904. doi:10.1074/jbc.M800340200

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Author Helland, Ronny
Fjellbirkeland, Anne
Karlsen, Odd Andre
Ve, Thomas
Lillehaug, Johan R.
Jensen, Harald B.
Title An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE
Formatted title
An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2008-05-16
Sub-type Article (original research)
DOI 10.1074/jbc.M800340200
Open Access Status File (Publisher version)
Volume 283
Issue 20
Start page 13897
End page 13904
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Proteins can coordinate metal ions with endogenous nitrogen and oxygen ligands through backbone amino and carbonyl groups, but the amino acid side chains coordinating metals do not include tryptophan. Here we show for the first time the involvement of the tryptophan metabolite kynurenine in a protein metal-binding site. The crystal structure to 1.35Å of MopE* from the methane-oxidizing Methylococcus capsulatus (Bath) provided detailed information about its structure and mononuclear copper-binding site. MopE* contains a novel protein fold of which only one-third of the structure displays similarities to other known folds. The geometry around the copper ion is distorted tetrahedral with one oxygen ligand from a water molecule, two histidine imidazoles (His-132 and His-203), and at the fourth distorted tetrahedral position, the N1 atom of the kynurenine, an oxidation product of Trp-130. Trp-130 was not oxidized to kynurenine in MopE* heterologously expressed in Escherichia coli, nor did this protein bind copper. Our findings indicate that the modification of tryptophan to kynurenine and its involvement in copper binding is an innate property of M. capsulatus MopE*.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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