Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery.

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 Lett

journal_title

FEBS letters

authors

Kitaoka S,Wada K,Hasegawa Y,Minami Y,Fukuyama K,Takahashi Y

doi

10.1016/j.febslet.2005.11.058

keywords:

subject

Has Abstract

pub_date

2006-01-09 00:00:00

pages

137-43

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)01429-8

journal_volume

580

pub_type

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