Počet záznamů: 1
Structural organization of WrbA in apo-and holoprotein crystals
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