2R96

Crystal structure of E. coli WrbA in complex with FMN

Summary for 2R96

• Entry DOI: 10.2210/pdb2r96/pdb
• Related: 2R97 2RG1
• Descriptor: Flavoprotein WrbA, FLAVIN MONONUCLEOTIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: electron transport, quinone oxidoreductase, flavoprotein, flavodoxin-like fold, fmn-binding, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 43506.59

Authors

Kuta Smatanova, I.,Wolfova, J.,Brynda, J.,Mesters, J.R.,Grandori, R.,Carey, J. (deposition date: 2007-09-12, release date: 2008-09-23, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)