2D3W

Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery

Summary for 2D3W

• Entry DOI: 10.2210/pdb2d3w/pdb
• Descriptor: Probable ATP-dependent transporter sufC (2 entities in total)
• Functional Keywords: abc-atpase, abc-transporter, iron-sulfur cluster, sufc, biosynthetic protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P77499
• Total number of polymer chains: 4
• Total formula weight: 110453.33

Authors

Kitaoka, S.,Wada, K.,Hasegawa, Y.,Minami, Y.,Takahashi, Y.,Fukuyama, K. (deposition date: 2005-10-03, release date: 2006-01-17, Last modification date: 2024-03-13)

Primary citation

Kitaoka, S.,Wada, K.,Hasegawa, Y.,Minami, Y.,Fukuyama, K.,Takahashi, Y.
Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery
Febs Lett., 580:137-143, 2006

PubMed 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.

PubMed: 16364320
DOI: 10.1016/j.febslet.2005.11.058

Experimental method

X-RAY DIFFRACTION (2.5 Å)