2R97

Crystal structure of E. coli WrbA in complex with FMN

2R97 の概要

• エントリーDOI: 10.2210/pdb2r97/pdb
• 関連するPDBエントリー: 2R96 2RG1
• 分子名称: Flavoprotein WrbA, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: electron transport, quinone oxidoreductase, flavoprotein, flavodoxin-like fold, fmn-binding, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42637.63

構造登録者

Kuta Smatanova, I.,Wolfova, J.,Brynda, J.,Mesters, J.R.,Grandori, R.,Carey, J. (登録日: 2007-09-12, 公開日: 2008-09-23, 最終更新日: 2023-08-30)

主引用文献

Wolfova, J.,Smatanova, I.K.,Brynda, J.,Mesters, J.R.,Lapkouski, M.,Kuty, M.,Natalello, A.,Chatterjee, N.,Chern, S.Y.,Ebbel, E.,Ricci, A.,Grandori, R.,Ettrich, R.,Carey, J.
Structural organization of WrbA in apo- and holoprotein crystals.
Biochim.Biophys.Acta, 1794:1288-1298, 2009

PubMed Abstract: Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 A resolution, and new crystals of WrbA apoprotein diffracting to 1.85 A, are refined and analysed comparatively through the lens of flavodoxin structures. The results indicate that differences between apo- and holoWrbA crystal structures are manifested on many levels of protein organization as well as in the FMN-binding sites. Evaluation of the influence of crystal contacts by comparison of lattice packing reveals the protein's global response to FMN binding. Structural changes upon cofactor binding are compared with the monomeric flavodoxins. Topologically non-equivalent residues undergo remarkably similar local structural changes upon FMN binding to WrbA or to flavodoxin, despite differences in multimeric organization and residue types at the binding sites. Analysis of the three crystal structures described here, together with flavodoxin structures, rationalizes functional similarities and differences of the WrbAs relative to flavodoxins, leading to a new understanding of the defining features of WrbAs. The results suggest that WrbAs are not a remote and unusual branch of the flavodoxin family as previously thought but rather a central member with unifying structural features.

PubMed: 19665595
DOI: 10.1016/j.bbapap.2009.08.001

実験手法

X-RAY DIFFRACTION (2 Å)