RmlC-like jelly roll fold QuickView

Description:: RmlC (deoxythymidine diphosphates-4-dehydrorhamnose 3,5-epimerase; ) is a mainly beta class protein with a jelly roll-like topology. It is a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. This entry represents the domain with the jelly roll-like fold. Other protein families containing this domain include glucose-6-phosphate isomerase ; germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities; auxin-binding protein; seed storage protein 7S; acireductone dioxygenase; as well as three proteins that have metal-binding sites similar to that of germine, namely quercetin 2,3-dioxygenase , phosphomannose isomerase and homogentisate dioxygenase , the last three sharing a 2-domain fold with storage protein 7s.The cAMP-binding domains found in the cAMP receptor protein (CRP) family display a similar beta-roll architecture consisting of eight antiparallel beta-strands and three helical segments. These proteins include CooA, a CO-sensing haem protein that functions as a transcription activator, and the CnbD (cyclic nucleotide binding domain) of the HCN cation channel in which cAMP binding modulates gating of the channel.