2vow
From Proteopedia
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'''AN OXIDIZED TRYPTOPHAN FACILITATES COPPER-BINDING IN METHYLOCOCCUS CAPSULATUS SECRETED PROTEIN MOPE. THE STUCTURE OF RECOMBINANT MOPE TO 1.65AA''' | '''AN OXIDIZED TRYPTOPHAN FACILITATES COPPER-BINDING IN METHYLOCOCCUS CAPSULATUS SECRETED PROTEIN MOPE. THE STUCTURE OF RECOMBINANT MOPE TO 1.65AA''' | ||
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| + | ==Overview== | ||
| + | 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 1.35A 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(*). | ||
==About this Structure== | ==About this Structure== | ||
2VOW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOW OCA]. | 2VOW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOW OCA]. | ||
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| + | ==Reference== | ||
| + | An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE., Helland R, Fjellbirkeland A, Karlsen OA, Ve T, Lillehaug JR, Jensen HB, J Biol Chem. 2008 May 16;283(20):13897-904. Epub 2008 Mar 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18348978 18348978] | ||
[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Oxidized tryptophan]] | [[Category: Oxidized tryptophan]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:33:20 2008'' |
Revision as of 19:33, 22 May 2008
AN OXIDIZED TRYPTOPHAN FACILITATES COPPER-BINDING IN METHYLOCOCCUS CAPSULATUS SECRETED PROTEIN MOPE. THE STUCTURE OF RECOMBINANT MOPE TO 1.65AA
Overview
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 1.35A 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(*).
About this Structure
2VOW is a Single protein structure of sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE., Helland R, Fjellbirkeland A, Karlsen OA, Ve T, Lillehaug JR, Jensen HB, J Biol Chem. 2008 May 16;283(20):13897-904. Epub 2008 Mar 18. PMID:18348978 Page seeded by OCA on Thu May 22 22:33:20 2008
