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MBOAT

The MBOAT family of membrane proteins is a family of various acyltransferase enzymes. All family members contain multiple transmembrane domains and most carry two conserved residues, a conserved histidine (His) embedded in a hydrophobic stretch of residues and an asparagine (Asn) or histidine within a more hydrophilic region some 30-50 residues upstream.

Structure
The structure for one MBOAT protein, DltB from Streptococcus thermophilus (), has been solved. DltB performs D-alanylation of cell-wall teichoic acid. It contains a ring of 11 transmembrane helices surrounding a tunnel that goes through the biological membrane. The tunnel connects to a partner, DltC, which carries the D-alanine to the conserved histidine residue of DltB MBOAT located at the bottom of the funnel. A computational model of human ghrelin O-acyltransferase (GOAT) (Q96T53) revealed a transmembrane channel that facilitates octanoylation of the peptide hormone ghrelin. DltB and GOAT share structural similarities in their homologous regions, suggesting a common core fold for MBOAT family members. == Human proteins with this domain ==
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