Structural organization of WrbA in apo- and holoprotein crystals

Julie Wolfova, Ivana Kuta Smatanova, Jiri Brynda, Jeroen R. Mesters, Mikalai Lapkouski, Michal Kuty, Antonino Natalello, Neal Chatterjee, Sy Yeu Chern, Erin Ebbel, Angela Ricci, Rita Grandori, Rüdiger Ettrich*, Jannette Carey

*Corresponding author for this work
10 Citations (Scopus)


Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 Å resolution, and new crystals of WrbA apoprotein diffracting to 1.85 Å, 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.

Original languageEnglish
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number9
Pages (from-to)1288-1298
Number of pages11
Publication statusPublished - 01.09.2009

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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