Počet záznamů: 1

Structural organization of WrbA in apo-and holoprotein crystals

  1. 1.
    0343396 - UOCHB-X 2011 RIV NL eng J - Článek v odborném periodiku
    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
    Grant CEP: GA MŠk(CZ) LC06010
    Výzkumný záměr: CEZ:AV0Z40550506; CEZ:AV0Z60870520
    Klíčová slova: twisted open-sheet fold * electrostatic potential surface * dimerization * trichloroacetic acid
    Kód oboru RIV: CC - Organická chemie
    Impakt faktor: 2.480, rok: 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.
    Trvalý link: http://hdl.handle.net/11104/0185886