@article{open1761,
          volume = {191},
          number = {3},
           month = {September},
          author = {Gurmeet Kaur and Srikrishna Subramanian},
            note = {Copyright of this article belongs to Elsevier Science.},
           title = {The Ku-Mar zinc finger: A segment-swapped zinc ribbon in MarR-like transcription regulators related to the Ku bridge.},
       publisher = {Elsevier Science},
            year = {2015},
         journal = {Journal of structural biology},
           pages = {281--9},
        keywords = {Zinc ribbon; 
Segment-swapping; 
DNA-binding proteins; 
Helix-turn-helix domain; 
Dimerization; 
Multidrug resistance
},
             url = {http://crdd.osdd.net/open/1761/},
        abstract = {Two putative oxidative-stress sensor proteins from Pseudomonas aeruginosa, PA1607 and PA1374, belong to the MarR family of transcription regulators and possess a unique mode of dimerization. In these proteins, in addition to the {\ensuremath{\alpha}}-helices involved in dimerization, inter-subunit contacts are strengthened by additional C-terminal {\ensuremath{\beta}}-strands. Using sequence and structure analysis we show that these {\ensuremath{\beta}}-strands constitute a novel segment-swapped zinc ribbon domain. We detect the presence of the zinc ribbon domain in MarR proteins from many bacterial homologs. While the metal-chelating residues of the zinc ribbons are absent in most members of this family, we could however identify several species of Proteobacteria, Actinobacteria and Firmicutes that possess intact zinc-chelating sites. Conservation pattern of metal-chelating residues together with the extensive structural resemblance to zinc ribbons, in particular to the bridge-region of the dsDNA break repair protein Ku, suggests that the C-terminal {\ensuremath{\beta}}-rich region of these proteins is a zinc ribbon. Sequence analysis also supports a distant evolutionary connection between the zinc ribbons of the MarR and Ku families. However, unlike Ku where the segment-swapped zinc ribbons play a role in DNA-binding and obligate dimerization, their primary role in MarR appears to be in dimerization and strengthening of inter-subunit contacts.}
}