By analyzing the pattern, chemists can deduce the structure of the protein molecules that make up the crystal. One region had an unusual topology and chemical characteristics that suggested it could be the place where the protein bound the RNA portion of the ribonuclease P enzyme. These findings were particularly surprising, said the chemists, because most theories held that such proteins played only a structural role, helping fold the RNA into its active form, and not an active role in the catalytic chemical reaction. This binding could have been either an indirect effect, like changing the conformation of the RNA, or a direct effect. And in general it's been believed such proteins were only involved in folding the RNA, and not really involved in catalysis.
P grab magnesium atoms that it needs to function optimally.
Such findings may offer intriguing insights into how the machinery of living cells first evolved, Fierke said. And RNA is not particularly good at forming specific metal binding sites, whereas proteins are particularly good. The biochemists' work might offer new targets for antibiotics, since ribonuclease P is essential for making all tRNAs, and since the bacterial enzyme is different from the enzyme in higher organisms. Contact the Webmaster .