Protein Family Models

Zn-ribbon_9 is a Zn-ribbon domain rich in aromatic and positively charged amino acid residues. This C-terminal Zn-ribbon domain consists of two beta-strands acting as a scaffold for the two Zn knuckles. Both pairs of cysteines making up the two Zn knuckles are situated at highly conserved sharp beta-turns, an arrangement that facilitates the tetrahedral coordination of the divalent Zn ion. The two Zn-knuckle cysteine motifs are separated by 20 residues, 9 of which form an alpha-helix (helix 4) [2].Structural modelling suggests this domain may bind nucleic acids [1]. The domain appears to bind flaA-mRNA, thus contributing to flagellum formation and motility [2]. [1]. 21348639. Ab Initio Modeling Led Annotation Suggests Nucleic Acid Binding Function for Many DUFs. Rigden DJ;. OMICS 2011;0:0-0. [2]. 20826163. The 2.2-A structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain. Caly DL, O'Toole PW, Moore SA;. J Mol Biol. 2010;403:405-419. (from Pfam)

Date:

2024-10-16

zinc ribbon domain-containing protein may bind nucleic acids; similar to Mycobacterium tuberculosis uncharacterized protein Rv2229c

Date:

2024-11-08