3EYY
Structural basis for the specialization of Nur, a nickel-specific Fur homologue, in metal sensing and DNA recognition
Summary for 3EYY
Entry DOI | 10.2210/pdb3eyy/pdb |
Descriptor | Putative iron uptake regulatory protein, NICKEL (II) ION, ZINC ION, ... (7 entities in total) |
Functional Keywords | nur, nickel-uptake regulator, d-domain, dimerization domain, db-domain, dna-binding domain, transport |
Biological source | Streptomyces coelicolor |
Total number of polymer chains | 2 |
Total formula weight | 33488.45 |
Authors | Cha, S.-S.,An, Y.J. (deposition date: 2008-10-22, release date: 2009-06-09, Last modification date: 2023-12-27) |
Primary citation | An, Y.J.,Ahn, B.-E.,Han, A.-R.,Kim, H.-M.,Chung, K.M.,Shin, J.-H.,Cho, Y.-B.,Roe, J.-H.,Cha, S.-S. Structural basis for the specialization of Nur, a nickel-specific Fur homolog, in metal sensing and DNA recognition Nucleic Acids Res., 37:3442-3451, 2009 Cited by PubMed Abstract: Nur, a member of the Fur family, is a nickel-responsive transcription factor that controls nickel homeostasis and anti-oxidative response in Streptomyces coelicolor. Here we report the 2.4-A resolution crystal structure of Nur. It contains a unique nickel-specific metal site in addition to a nonspecific common metal site. The identification of the 6-5-6 motif of the Nur recognition box and a Nur/DNA complex model reveals that Nur mainly interacts with terminal bases of the palindrome on complex formation. This contrasts with more distributed contacts between Fur and the n-1-n type of the Fur-binding motif. The disparity between Nur and Fur in the conformation of the S1-S2 sheet in the DNA-binding domain can explain their different DNA-recognition patterns. Furthermore, the fact that the specificity of Nur in metal sensing and DNA recognition is conferred by the specific metal site suggests that its introduction drives the evolution of Nur orthologs in the Fur family. PubMed: 19336416DOI: 10.1093/nar/gkp198 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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