2VOV
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA
2VOV の概要
| エントリーDOI | 10.2210/pdb2vov/pdb |
| 関連するPDBエントリー | 2VOW 2VOX |
| 分子名称 | SURFACE-ASSOCIATED PROTEIN, CALCIUM ION, COPPER (II) ION, ... (4 entities in total) |
| 機能のキーワード | metal-binding protein, oxidized tryptophan, methanotroph bacterium, kunurenine, copper homeostasis, metal binding protein |
| 由来する生物種 | METHYLOCOCCUS CAPSULATUS |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 36289.46 |
| 構造登録者 | Helland, R.,Fjellbirkeland, A.,Karlsen, O.A.,Ve, T.,Lillehaug, J.R.,Jensen, H.B. (登録日: 2008-02-22, 公開日: 2008-03-18, 最終更新日: 2024-10-23) |
| 主引用文献 | Helland, R.,Fjellbirkeland, A.,Karlsen, O.A.,Ve, T.,Lillehaug, J.R.,Jensen, H.B. An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus Capsulatus-Secreted Protein Mope. J.Biol.Chem., 283:13897-, 2008 Cited by PubMed 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 1.35 angstroms 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*. PubMed: 18348978DOI: 10.1074/JBC.M800340200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.35 Å) |
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