Structural organization of WrbA in apo-and holoprotein crystals

0343396 - ÚOCHB 2011 RIV NL eng J - Journal Article
Wolfová, J. - Kutá-Smatanová, Ivana - Brynda, Jiří - Mesters, J. R. - Lapkouski, M. - Kutý, Michal - Natalello, A. - Chatterjee, N. - Chern, S. Y. - Ebbel, E. - Ricci, A. - Grandori, R. - Ettrich, Rüdiger - Carey, J.
Structural organization of WrbA in apo-and holoprotein crystals.
Biochimica Et Biophysica Acta-Proteins and Proteomics. Roč. 1794, č. 9 (2009), s. 1288-1298. ISSN 1570-9639. E-ISSN 1878-1454
R&D Projects: GA MŠMT(CZ) LC06010
Institutional research plan: CEZ:AV0Z40550506; CEZ:AV0Z60870520
Keywords : twisted open-sheet fold * electrostatic potential surface * dimerization * trichloroacetic acid
Subject RIV: CC - Organic Chemistry
Impact factor: 2.480, year: 2009

Crystal structure of /E. coli/ protein WrbA holoprotein to 2.6 and 2.0 Å resolution, and WrbA apoprotein 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. Structural changes upon cofactor binding are compared with the monomeric flavodoxins. 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.
Permanent Link: http://hdl.handle.net/11104/0185886