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The C-terminal DNA-binding domain of OmpR, a positive regulator involved in osmoregulation expression of the ompF and ompC genes in Escherichia coli, has a helix-turn-helix variant motif. The ‘turn’ region, consisting of 11 residues, forms an RNA polymerase contact site.
Transfection studies with cDNAs encoding hybrids between the highly similar cytochrome P450 enzymes, CYP11B1 (steroid 11β-hydroxylase) and CYP11B2 (aldosterone synthase) have identified which amino acids determine the different activities of the enzymes.
The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates.