Počet záznamů: 1
Structural organization of WrbA in apo- and holoprotein crystals
0341145 - UEK-B 2010 RIV NL eng J - Článek v odborném periodiku
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:AV0Z60870520
Klíčová slova: Dimerization * Diffraction resolution
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.480, rok: 2009
Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 angstrom resolution, and new crystals of WrbA apoprotein diffracting to 1.85 angstrom, 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.
Trvalý link: http://hdl.handle.net/11104/0184222