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

Wolfova, J., Smatanova, I., Brynda, J., Mesters, J., Lapkouski, M., Kuty, M., et al. (2009). Structural organization of WrbA in apo- and holoprotein crystals. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1794(9), 1288-1298 [10.1016/j.bbapap.2009.08.001].

Structural organization of WrbA in apo- and holoprotein crystals

NATALELLO, ANTONINO;GRANDORI, RITA;
2009

Abstract

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
Articolo in rivista - Articolo scientifico
Twisted open-sheet fold; Electrostatic potential surface; Dimerization; Trichloroacetic acid; Disulfide; NAD(P)H:quinone oxidoreductase; Diffraction resolution
English
1288
1298
11
Wolfova, J., Smatanova, I., Brynda, J., Mesters, J., Lapkouski, M., Kuty, M., et al. (2009). Structural organization of WrbA in apo- and holoprotein crystals. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1794(9), 1288-1298 [10.1016/j.bbapap.2009.08.001].
Wolfova, J; Smatanova, I; Brynda, J; Mesters, J; Lapkouski, M; Kuty, M; Natalello, A; Chatterjee, N; Chern, S; Ebbel, E; Ricci, A; Grandori, R; Ettrich, R; Carey, J
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/9369
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