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2d3w
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(New page: 200px<br /><applet load="2d3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d3w, resolution 2.5Å" /> '''Crystal Structure of ...)
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Revision as of 07:18, 21 November 2007
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Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery
Overview
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.
About this Structure
2D3W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery., Kitaoka S, Wada K, Hasegawa Y, Minami Y, Fukuyama K, Takahashi Y, FEBS Lett. 2006 Jan 9;580(1):137-43. Epub 2005 Dec 6. PMID:16364320
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