PMID:16364320

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Citation

Kitaoka, S, Wada, K, Hasegawa, Y, Minami, Y, Fukuyama, K and Takahashi, Y (2006) Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery. FEBS Lett. 580:137-43

Abstract

SufC is an ATPase component of the SUF machinery, which is involved in the biosynthesis of Fe-S clusters. To gain insight into the function of this protein, we have determined the crystal structure of Escherichia coli SufC at 2.5A resolution. Despite the similarity of the overall structure with ABC-ATPases (nucleotide-binding domains of ABC transporters), some key differences were observed. Glu171, an invariant residue involved in ATP hydrolysis, is rotated away from the nucleotide-binding pocket to form a SufC-specific salt bridge with Lys152. Due to this salt bridge, D-loop that follows Glu171 is flipped out to the molecular surface, which may sterically inhibit the formation of an active dimer. Thus, the salt bridge may play a critical role in regulating ATPase activity and preventing wasteful ATP hydrolysis. Furthermore, SufC has a unique Q-loop structure on its surface, which may form a binding site for its partner proteins, SufB and/or SufD.

Links

PubMed Online version:10.1016/j.febslet.2005.11.058

Keywords

ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/metabolism; Absorptiometry, Photon; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Binding Sites; Dimerization; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Glutamine/chemistry; Glutamine/metabolism; Iron/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Sulfur/metabolism

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