Details

Autor(en) / Beteiligte

• Dutta, Samit Kumar
• Serrano, Pedro
• Geralt, Michael
• Axelrod, Herbert L.
• Xu, Qingping
• Lesley, Scott A.
• Godzik, Adam
• Deacon, Ashley M.
• Elsliger, Marc‐André
• Wilson, Ian A.
• Wüthrich, Kurt

Titel

Cofactor‐induced reversible folding of Flavodoxin‐4 from Lactobacillus acidophilus

Ist Teil von

• Protein science, 2015-10, Vol.24 (10), p.1600-1608

Ort / Verlag

United States: Wiley Subscription Services, Inc

Erscheinungsjahr

2015

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• Flavodoxins in combination with the flavin mononucleotide (FMN) cofactor play important roles for electron transport in prokaryotes. Here, novel insights into the FMN‐binding mechanism to flavodoxins‐4 were obtained from the NMR structures of the apo‐protein from Lactobacillus acidophilus (YP_193882.1) and comparison of its complex with FMN. Extensive reversible conformational changes were observed upon FMN binding and release. The NMR structure of the FMN complex is in agreement with the crystal structure (PDB ID: 3EDO) and exhibits the characteristic flavodoxin fold, with a central five‐stranded parallel β–sheet and five α‐helices forming an α/β‐sandwich architecture. The structure differs from other flavoproteins in that helix α2 is oriented perpendicular to the β‐sheet and covers the FMN‐binding site. This helix reversibly unfolds upon removal of the FMN ligand, which represents a unique structural rearrangement among flavodoxins.