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beta-barrel domain of carboxypeptidase M99 This is the central, beta-barrel, domain of the metallo-carboxypeptidase that maintains helical cell-shape in Helicobacter. It shows a novel fold. It has a highly positively charged surface which contributes to a high overall isoelectric point. A calcium-binding channel is formed from residues in the C-terminal Ig-like domain in conjunction with some of the long side-chains of residues from strands beta-14 and beta-18 of this domain.
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PubMed References
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Jiyao W et al.(2023). "The conserved domain database in 2023.",