2d2f
Crystal structure of atypical cytoplasmic ABC-ATPase SufC from Thermus thermophilus HB8
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OverviewOverview
SufC, a cytoplasmic ABC-ATPase, is one of the most conserved Suf proteins., SufC forms a stable complex with SufB and SufD, and the SufBCD complex, interacts with other Suf proteins in the Fe-S cluster assembly. We have, determined the crystal structure of SufC from Thermus thermophilus HB8 in, nucleotide-free and ADP-Mg-bound states at 1.7A and 1.9A resolution, respectively. The overall architecture of the SufC structure is similar to, other ABC ATPases structures, but there are several specific motifs in, SufC. Three residues following the end of the Walker B motif form a novel, 3(10) helix which is not observed in other ABC ATPases. Due to the novel, 3(10) helix, a conserved glutamate residue involved in ATP hydrolysis is, flipped out. Although this unusual conformation is unfavorable for ATP, hydrolysis, salt-bridges formed by conserved residues and a strong, hydrogen-bonding network around the novel 3(10) helix suggest that the, novel 3(10) helix of SufC is a rigid conserved motif. Compared to other, ABC-ATPase structures, a significant displacement occurs at a linker, region between the ABC alpha/beta domain and the alpha-helical domain. The, linker conformation is stabilized by a hydrophobic interaction between, conserved residues around the Q loop. The molecular surfaces of SufC and, the C-terminal helices of SufD (PDB code: 1VH4) suggest that the unusual, linker conformation conserved among SufC proteins is probably suitable for, interacting with SufB and SufD.
About this StructureAbout this Structure
2D2F is a Single protein structure of sequence from Thermus thermophilus with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of atypical cytoplasmic ABC-ATPase SufC from Thermus thermophilus HB8., Watanabe S, Kita A, Miki K, J Mol Biol. 2005 Nov 11;353(5):1043-54. Epub 2005 Sep 23. PMID:16216272
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