1R95
Crystal Structure of IscA (native)
Summary for 1R95
| Entry DOI | 10.2210/pdb1r95/pdb |
| Related | 1R94 |
| Descriptor | Protein yfhF (2 entities in total) |
| Functional Keywords | tetrameric, beta barrel, iron-sulfur cluster protein, pseudo-asymmetric motifs, metal transport |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 25686.88 |
| Authors | Bilder, P.W.,Ding, H.,Newcomer, M.E. (deposition date: 2003-10-28, release date: 2003-12-23, Last modification date: 2024-02-14) |
| Primary citation | Bilder, P.W.,Ding, H.,Newcomer, M.E. Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry, 43:133-139, 2004 Cited by PubMed 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. PubMed: 14705938PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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