PMID:14705938

Citation	Bilder, PW, Ding, H and Newcomer, ME (2004) Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry 43:133-9
Abstract	IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain. In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU, a protein which is thought to have a similar function, the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold. However, the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure. In addition, the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.
Links	PubMed Online version:10.1021/bi035440s
Keywords	Amino Acid Sequence; Animals; Conserved Sequence; Crystallization; Crystallography, X-Ray; Cysteine/chemistry; Cysteine/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Humans; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/metabolism; Mice; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; Sequence Alignment
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