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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kitaoka S,Wada K,Hasegawa Y,Minami Y,Fukuyama K,Takahashi Ydoi
10.1016/j.febslet.2005.11.058keywords:
subject
Has Abstractpub_date
2006-01-09 00:00:00pages
137-43issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(05)01429-8journal_volume
580pub_type
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