Crystal Structure of Escherichia Coli Sufc, an Abc-type Atpase Component of the Suf Iron-sulfur Cluster Assembly Machinery.
From: Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
FEBS letters
- Publish Date: Jan 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 1
- Pages: 137-43
- Medium: Print
- Language: English
- Citation (JAMA): Kitaoka Shintaro, Wada Kei, Hasegawa Yuko, et al. Crystal Structure of Escherichia Coli Sufc, an Abc-type Atpase Component of the Suf Iron-sulfur Cluster Assembly Machinery.. FEBS Lett. Jan 2006;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.
Mesh Headings (Keywords): ATP-Binding Cassette Transporters, Absorptiometry, Photon, Adenosine Triphosphatases, Binding Sites, Dimerization, Escherichia coli, Escherichia coli Proteins, Glutamine, Iron, Protein Structure, Secondary, Protein Structure, Tertiary, Sulfur
Check for Full Text / PubMed Unique Identifier (PMID): 16364320
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