5G5H
Escherichia coli Periplasmic Aldehyde Oxidase R440H mutant
5G5H の概要
| エントリーDOI | 10.2210/pdb5g5h/pdb |
| 関連するPDBエントリー | 5G5G |
| 分子名称 | Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA, PTERIN CYTOSINE DINUCLEOTIDE, DIOXOTHIOMOLYBDENUM(VI) ION, ... (13 entities in total) |
| 機能のキーワード | oxidoreductase, paoabc, xanthine oxidase family, heterotrimer, e.coli detoxification |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 140602.23 |
| 構造登録者 | Correia, M.A.S.,Otrelo-Cardoso, A.R.,Romao, M.J.,Santos-Silva, T. (登録日: 2016-05-25, 公開日: 2016-09-28, 最終更新日: 2024-10-23) |
| 主引用文献 | Correia, M.A.,Otrelo-Cardoso, A.R.,Schwuchow, V.,Sigfridsson Clauss, K.G.,Haumann, M.,Romao, M.J.,Leimkuhler, S.,Santos-Silva, T. The Escherichia Coli Periplasmic Aldehyde Oxidoreductase is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes. Acs Chem.Biol., 11:2923-, 2016 Cited by PubMed Abstract: The xanthine oxidase (XO) family comprises molybdenum-dependent enzymes that usually form homodimers (or dimers of heterodimers/trimers) organized in three domains that harbor two [2Fe-2S] clusters, one FAD, and a Mo cofactor. In this work, we crystallized an unusual member of the family, the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli. This is the first example of an E. coli protein containing a molybdopterin-cytosine-dinucleotide cofactor and is the only heterotrimer of the XO family so far structurally characterized. The crystal structure revealed the presence of an unexpected [4Fe-4S] cluster, anchored to an additional 40 residues subdomain. According to phylogenetic analysis, proteins containing this cluster are widely spread in many bacteria phyla, putatively through repeated gene transfer events. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (PaoC-R440) making a direct interaction with PaoC-E692, which acts as a base catalyst. In order to understand the importance of R440, kinetic assays were carried out, and the crystal structure of the PaoC-R440H variant was also determined. PubMed: 27622978DOI: 10.1021/ACSCHEMBIO.6B00572 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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